3qy6: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 9: Line 9:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qy6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qy6 RCSB], [http://www.ebi.ac.uk/pdbsum/3qy6 PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qy6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qy6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qy6 RCSB], [http://www.ebi.ac.uk/pdbsum/3qy6 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/YWQE_BACSU YWQE_BACSU]] Dephosphorylates the phosphotyrosine-containing proteins YwqD, YwqF and Ssb.<ref>PMID:16549871</ref> 
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 20:54, 25 December 2014

Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatasesCrystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases

Structural highlights

3qy6 is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:BSU36240, ywqE (Bacillus subtilis)
Activity:Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[YWQE_BACSU] Dephosphorylates the phosphotyrosine-containing proteins YwqD, YwqF and Ssb.[1]

Publication Abstract from PubMed

Unique metal-dependent protein tyrosine phosphatases that belong to the polymerase and histindinol phosphatase (PHP) family are present in Gram-positive bacteria. They are distinct from the Cys-based, low-molecular-weight phosphotyrosine protein phosphatases (LMPTPs). Two representative members of the PHP family tyrosine phosphatases are YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae. YwqE is involved in polysaccharide biosynthesis, bacterial DNA metabolism, and DNA damage response in B. subtilis. CpsB regulates capsular polysaccharide biosynthesis via tyrosine dephosphorylation of CpsD, its cognate tyrosine kinase, in S. pneumoniae. To gain insights into the active site and possible conformational changes of the metal-dependent tyrosine phosphatases from Gram-positive bacteria, we have determined the crystal structures of B. subtilis YwqE (in both the apo form and the phosphate-bound form) and S. pneumoniae CpsB (in the sulfate-bound form). Comparisons of the three structures reveal conformational plasticity of two active site loops. Furthermore, in both structures of the phosphate-bound YwqE and the sulfate-bound CpsB, the phosphate (or sulfate) ion is bound to a cluster of three metal ions in the active site, thus providing insight into the pre-catalytic state.

Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases.,Kim HS, Lee SJ, Yoon HJ, An DR, Kim DJ, Kim SJ, Suh SW J Struct Biol. 2011 May 14. PMID:21605684[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Mijakovic I, Petranovic D, Macek B, Cepo T, Mann M, Davies J, Jensen PR, Vujaklija D. Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine. Nucleic Acids Res. 2006 Mar 20;34(5):1588-96. Print 2006. PMID:16549871 doi:http://dx.doi.org/34/5/1588
  2. Kim HS, Lee SJ, Yoon HJ, An DR, Kim DJ, Kim SJ, Suh SW. Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases. J Struct Biol. 2011 May 14. PMID:21605684 doi:10.1016/j.jsb.2011.05.007

3qy6, resolution 1.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA