Phosphatase Superfamily CC2 - Revision history

Mark: /* Phosphatase domain structure */

2015-11-16T21:34:19Z

‎Phosphatase domain structure

Mark at 07:36, 15 November 2015

2015-11-15T07:36:20Z

Mark: /* Phosphatase domain structure */

2015-11-15T07:34:06Z

‎Phosphatase domain structure

Mark: /* Phosphatase domain structure */

2015-11-15T07:32:48Z

‎Phosphatase domain structure

Mark: /* Phosphatase domain structure */

2015-11-15T07:30:59Z

‎Phosphatase domain structure

Mark at 06:22, 15 November 2015

2015-11-15T06:22:09Z

Gerard at 04:41, 31 May 2015

2015-05-31T04:41:31Z

Mark at 23:02, 31 December 2014

2014-12-31T23:02:14Z

Gerard at 20:24, 6 December 2014

2014-12-06T20:24:10Z

Gerard: Created page with "NOTOC Phosphatase Classification: Superfamily CC2 This superfamily has a unique fold, but shares the common..."

2014-12-06T20:23:03Z

Created page with "__NOTOC__ Phosphatase Classification: Superfamily CC2 This superfamily has a unique fold, but shares the common..."

New page

__NOTOC__
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Superfamily_CC2|Superfamily CC2]]

This superfamily has a unique fold, but shares the common CX5R catalytic motif with another two cysteine-based superfamilies, [[Phosphatase_Superfamily_CC1|superfamily CC1]] and [[Phosphatase_Superfamily_CC2|superfamily CC2]].

The superfamily consists of two member families present in human [[Phosphatase_Family_LMWPTP|low molecular weight PTP (LWMPTP)]] and [[Phosphatase_Family_SSU72|SSU72]]. Despite having only 15% sequence identity, human LMWPTP and SSU72 structures superimpose with an rmsd of 1.7 Å <cite>zhangy11</cite>.

A third family, arsenate reductase ([[Phosphatase_Family_ArsC|ArsC]]) <cite>Bennett</cite>, is only found in prokaryotes. While known to reduce arsenate to arsenite (a similar reaction to the phosphatase reaction), the B. subtilis gene also has in vitro phosphatase activity. A different phosphatase fold, CDC25/Rhodanese also has members in plants and yeast (ACR2) that are capable of arsenate reductase activity, highlighting the similarity of the protein phosphatase and arsenate reductase activities.

== Reference ==
<biblio>
#zhangy11 pmid=21204787
#Bennett pmid=11698660
</biblio>

@@ Line 8: / Line 8: @@
 The CC2 fold/superfamily shares the common CX5R catalytic motif with another two cysteine-based superfamilies, [[Phosphatase_Superfamily_CC1|CC1]] and [[Phosphatase_Superfamily_CC3|CC3]].
-The two families of CC2 fold/superfamily, [[Phosphatase_Family_LMWPTP|LWMPTP]] and [[Phosphatase_Family_SSU72|SSU72]], share a common fold, a 4-stranded beta sheet sided by helices, in a secondary structure combination of EHEHEHEH in sequence (numbered as E1, H1, E2, H4, E5, H5, E6, H6). The SSU72 family has an inserted 2-stranded beta sheet followed by two helices between E2 and H4, which are numbered as E3, E4, H2 and H3, respectively. The SSU72 family also has a helix and a beta strand at C terminus. The beta strand form the beta sheet with E1, E2, E5, E6. In other words, The LWMPTP family has a secondary structure combination of E1, H1, E2, H4, E5, H5, E6, H6. The SSU72 family has a secondary structure combination of E1, H1, E2, E3, E4, H2, H3, H4, E5, H5, E6, H6, H7, E7.
+The two families of CC2 fold/superfamily, [[Phosphatase_Family_LMWPTP|LMWPTP]] and [[Phosphatase_Family_SSU72|SSU72]], share a common fold, a 4-stranded beta sheet sided by helices, in a secondary structure combination of EHEHEHEH in sequence (numbered as E1, H1, E2, E5, H5, E6, H6). The beta strand form the beta sheet with E1, E2, E5, E6.
 The LMWPTP family is similar to CC1 fold in the following aspects, while the SSU72 family is more distinct from CC1 fold:

@@ Line 1: / Line 1: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC2|Fold CC2]]: [[Phosphatase_Superfamily_CC2|Superfamily CC2]]
 CC2 consists of two member families in human [[Phosphatase_Family_LMWPTP|low molecular weight PTP (LWMPTP)]] and [[Phosphatase_Family_SSU72|SSU72]]. Despite having only 15% sequence identity, human LMWPTP and SSU72 structures superimpose with an rmsd of 1.7 Å <cite>zhangy11</cite>.
@@ Line 8: / Line 6: @@
 == Phosphatase domain structure ==
-The two families [[Phosphatase_Family_LMWPTP|LWMPTP]] and [[Phosphatase_Family_SSU72|SSU72]] share a common fold, a 4-stranded beta sheet sided by helices, in a secondary structure combination of EHEHEHEH in sequence (numbered as E1, H1, E2, H4, E5, H5, E6, H6). The SSU72 family has an inserted 2-stranded beta sheet followed by two helices between E2 and H4, which are numbered as E3, E4, H2 and H3, respectively. The SSU72 family also has a helix and a beta strand at C terminus. The beta strand form the beta sheet with E1, E2, E5, E6. In other words, The LWMPTP family has a secondary structure combination of E1, H1, E2, H4, E5, H5, E6, H6. The SSU72 family has a secondary structure combination of E1, H1, E2, E3, E4, H2, H3, H4, E5, H5, E6, H6, H7, E7.
+The CC2 fold/superfamily shares the common CX5R catalytic motif with another two cysteine-based superfamilies, [[Phosphatase_Superfamily_CC1|CC1]] and [[Phosphatase_Superfamily_CC3|CC3]].
 The LMWPTP family is similar to CC1 fold in the following aspects, while the SSU72 family is more distinct from CC1 fold:

@@ Line 10: / Line 10: @@
 The two families [[Phosphatase_Family_LMWPTP|LWMPTP]] and [[Phosphatase_Family_SSU72|SSU72]] share a common fold, a 4-stranded beta sheet sided by helices, in a secondary structure combination of EHEHEHEH in sequence (numbered as E1, H1, E2, H4, E5, H5, E6, H6). The SSU72 family has an inserted 2-stranded beta sheet followed by two helices between E2 and H4, which are numbered as E3, E4, H2 and H3, respectively. The SSU72 family also has a helix and a beta strand at C terminus. The beta strand form the beta sheet with E1, E2, E5, E6. In other words, The LWMPTP family has a secondary structure combination of E1, H1, E2, H4, E5, H5, E6, H6. The SSU72 family has a secondary structure combination of E1, H1, E2, E3, E4, H2, H3, H4, E5, H5, E6, H6, H7, E7.
-The LMWPTP family is similar to CC1 fold in the following aspects:
+The LMWPTP family is similar to CC1 fold in the following aspects, while the SSU72 family is more distinct from CC1 fold:
 * The beta sheet. The CC2 fold has a beta sheet formed by E1, E2, E5, E6 (and E7 in SSU72 family); The CC1 fold has a beta sheet formed by E2, E3, E4, E11, E12. The CC2 fold E1, E2, E5 and E6 resemble the CC1 fold E3, E4, E11 and E12, while CC2 E7 and CC1 E2 are at different sides of the beta sheet.
 * CC2 H1 and CC1 H4.

@@ Line 10: / Line 10: @@
 The two families [[Phosphatase_Family_LMWPTP|LWMPTP]] and [[Phosphatase_Family_SSU72|SSU72]] share a common fold, a 4-stranded beta sheet sided by helices, in a secondary structure combination of EHEHEHEH in sequence (numbered as E1, H1, E2, H4, E5, H5, E6, H6). The SSU72 family has an inserted 2-stranded beta sheet followed by two helices between E2 and H4, which are numbered as E3, E4, H2 and H3, respectively. The SSU72 family also has a helix and a beta strand at C terminus. The beta strand form the beta sheet with E1, E2, E5, E6. In other words, The LWMPTP family has a secondary structure combination of E1, H1, E2, H4, E5, H5, E6, H6. The SSU72 family has a secondary structure combination of E1, H1, E2, E3, E4, H2, H3, H4, E5, H5, E6, H6, H7, E7.
-In comparison with CC1 fold, the two folds resemble each other in the following aspects:
+The LMWPTP family is similar to CC1 fold in the following aspects:
 * The beta sheet. The CC2 fold has a beta sheet formed by E1, E2, E5, E6 (and E7 in SSU72 family); The CC1 fold has a beta sheet formed by E2, E3, E4, E11, E12. The CC2 fold E1, E2, E5 and E6 resemble the CC1 fold E3, E4, E11 and E12, while CC2 E7 and CC1 E2 are at different sides of the beta sheet.
 * CC2 H1 and CC1 H4.

@@ Line 8: / Line 8: @@
 == Phosphatase domain structure ==
-The two families [[Phosphatase_Family_LMWPTP|LWMPTP]] and [[Phosphatase_Family_SSU72|SSU72]] has a common fold.
+The two families [[Phosphatase_Family_LMWPTP|LWMPTP]] and [[Phosphatase_Family_SSU72|SSU72]] share a common fold, a 4-stranded beta sheet sided by helices, in a secondary structure combination of EHEHEHEH in sequence (numbered as E1, H1, E2, H4, E5, H5, E6, H6). The SSU72 family has an inserted 2-stranded beta sheet followed by two helices between E2 and H4, which are numbered as E3, E4, H2 and H3, respectively. The SSU72 family also has a helix and a beta strand at C terminus. The beta strand form the beta sheet with E1, E2, E5, E6. In other words, The LWMPTP family has a secondary structure combination of E1, H1, E2, H4, E5, H5, E6, H6. The SSU72 family has a secondary structure combination of E1, H1, E2, E3, E4, H2, H3, H4, E5, H5, E6, H6, H7, E7.
-The SSU72 family has a secondary structure combination of E1, H1, E2, E3, E4, H2, H3, H4, E5, H5, E6, H6, H7, E7.
+In comparison with CC1 fold, the two folds resemble each other in the following aspects:
+* The beta sheet. The CC2 fold has a beta sheet formed by E1, E2, E5, E6 (and E7 in SSU72 family); The CC1 fold has a beta sheet formed by E2, E3, E4, E11, E12. The CC2 fold E1, E2, E5 and E6 resemble the CC1 fold E3, E4, E11 and E12, while CC2 E7 and CC1 E2 are at different sides of the beta sheet.
-The LWMPTP family has a secondary structure combination of E1, H1, E2, H4 (or H3), E5, H5, E6, H6.
+* CC2 H1 and CC1 H4.
 == References ==

@@ Line 1: / Line 1: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC2|Fold CC2]]: [[Phosphatase_Superfamily_CC2|Superfamily CC2]]
@@ Line 8: / Line 7: @@
 A third family, arsenate reductase ([[Phosphatase_Family_ArsC|ArsC]]) <cite>Bennett</cite>, is only found in prokaryotes. While known to reduce arsenate to arsenite (a similar reaction to the phosphatase reaction), the B. subtilis gene also has in vitro phosphatase activity. A different phosphatase fold, CDC25/Rhodanese also has members in plants and yeast (ACR2) that are capable of arsenate reductase activity, highlighting the similarity of the protein phosphatase and arsenate reductase activities.
-== Reference ==
+== Phosphatase domain structure ==
 <biblio>
 #zhangy11 pmid=21204787
 #Bennett pmid=11698660
 </biblio>

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC2|Fold CC2]]: [[Phosphatase_Superfamily_CC2|Superfamily CC2]]
-This superfamily has a unique fold, but shares the common CX5R catalytic motif with another two cysteine-based superfamilies, [[Phosphatase_Superfamily_CC1|CC1]] and [[superfamily CC3]].
+This superfamily has a unique fold, but shares the common CX5R catalytic motif with another two cysteine-based superfamilies, [[Phosphatase_Superfamily_CC1|CC1]] and [[Phosphatase_Superfamily_CC3|CC3]].
-The superfamily consists of two member families present in human [[Phosphatase_Family_LMWPTP|low molecular weight PTP (LWMPTP)]] and [[Phosphatase_Family_SSU72|SSU72]]. Despite having only 15% sequence identity, human LMWPTP and SSU72 structures superimpose with an rmsd of 1.7 Å <cite>zhangy11</cite>.
+CC2 consists of two member families in human [[Phosphatase_Family_LMWPTP|low molecular weight PTP (LWMPTP)]] and [[Phosphatase_Family_SSU72|SSU72]]. Despite having only 15% sequence identity, human LMWPTP and SSU72 structures superimpose with an rmsd of 1.7 Å <cite>zhangy11</cite>.
 A third family, arsenate reductase ([[Phosphatase_Family_ArsC|ArsC]]) <cite>Bennett</cite>, is only found in prokaryotes. While known to reduce arsenate to arsenite (a similar reaction to the phosphatase reaction), the B. subtilis gene also has in vitro phosphatase activity. A different phosphatase fold, CDC25/Rhodanese also has members in plants and yeast (ACR2) that are capable of arsenate reductase activity, highlighting the similarity of the protein phosphatase and arsenate reductase activities.

Phosphatase Superfamily CC2 - Revision history

Mark: /* Phosphatase domain structure */

Mark at 07:36, 15 November 2015

Mark: /* Phosphatase domain structure */

Mark: /* Phosphatase domain structure */

Mark: /* Phosphatase domain structure */

Mark at 06:22, 15 November 2015

Gerard at 04:41, 31 May 2015

Mark at 23:02, 31 December 2014

Gerard at 20:24, 6 December 2014

Gerard: Created page with "__NOTOC__ Phosphatase Classification: Superfamily CC2 This superfamily has a unique fold, but shares the common..."

Gerard: Created page with "NOTOC Phosphatase Classification: Superfamily CC2 This superfamily has a unique fold, but shares the common..."