Difference between revisions of "Phosphatase Superfamily Cys-based III"
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This superfamily has a unique fold, but shares the common CX5R catalytic motif with another two cysteine-based superfamilies, [[Phosphatase_Superfamily_Cys-based_I|superfamily Cys-based I]] and [[Phosphatase_Superfamily_Cys-based_II|superfamily Cys-based II]]. | This superfamily has a unique fold, but shares the common CX5R catalytic motif with another two cysteine-based superfamilies, [[Phosphatase_Superfamily_Cys-based_I|superfamily Cys-based I]] and [[Phosphatase_Superfamily_Cys-based_II|superfamily Cys-based II]]. | ||
| − | The superfamily consists of two member families present in human [[Phosphatase_Family_LMWPTP|low molecular weight PTP (LWMPTP)]] and [[Phosphatase_Family_SSU72|SSU72]]. | + | 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 (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 == | == Reference == | ||
<biblio> | <biblio> | ||
#zhangy11 pmid=21204787 | #zhangy11 pmid=21204787 | ||
| + | #Bennett pmid=11698660 | ||
</biblio> | </biblio> | ||
Revision as of 23:34, 26 May 2014
Phosphatase Classification: Superfamily Cys-based III
This superfamily has a unique fold, but shares the common CX5R catalytic motif with another two cysteine-based superfamilies, superfamily Cys-based I and superfamily Cys-based II.
The superfamily consists of two member families present in human low molecular weight PTP (LWMPTP) and SSU72. Despite having only 15% sequence identity, human LMWPTP and SSU72 structures superimpose with an rmsd of 1.7 Å [1].
A third family, arsenate reductase (ArsC) [2], 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
- Zhang Y, Zhang M, and Zhang Y. Crystal structure of Ssu72, an essential eukaryotic phosphatase specific for the C-terminal domain of RNA polymerase II, in complex with a transition state analogue. Biochem J. 2011 Mar 15;434(3):435-44. DOI:10.1042/BJ20101471 |
- Bennett MS, Guan Z, Laurberg M, and Su XD. Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13577-82. DOI:10.1073/pnas.241397198 |
