Difference between revisions of "Phosphatase Superfamily CC2"
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== Phosphatase domain structure == | == Phosphatase domain structure == | ||
| − | The two families [[Phosphatase_Family_LMWPTP|LWMPTP]] and [[Phosphatase_Family_SSU72|SSU72]] | + | 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 | + | 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 | + | * CC2 H1 and CC1 H4. |
| + | * The catalytic motif locates between E1 and H1 in CC2 fold, and between E12 and H4 in CC1 fold. | ||
== References == | == References == | ||
Revision as of 07:30, 15 November 2015
Phosphatase Classification: Fold CC2: Superfamily CC2
This superfamily has a unique fold, but shares the common CX5R catalytic motif with another two cysteine-based superfamilies, CC1 and CC3.
CC2 consists of two member families 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.
Phosphatase domain structure
The two families LWMPTP and 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 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.
- The catalytic motif locates between E1 and H1 in CC2 fold, and between E12 and H4 in CC1 fold.
References
- 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 |
