3QY6

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

Summary for 3QY6

• Entry DOI: 10.2210/pdb3qy6/pdb
• Related: 3QY7 3QY8
• Descriptor: Tyrosine-protein phosphatase YwqE, FE (III) ION, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: tim barrel, polymerase and histindinol phosphatase(php)-like phosphatase, phosphatase, hydrolase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 30206.36

Authors

Kim, H.S.,Lee, S.J.,Yoon, H.J.,An, D.R.,Kim, D.J.,Kim, S.-J.,Suh, S.W. (deposition date: 2011-03-03, release date: 2011-06-08, Last modification date: 2024-02-21)

Primary citation

Kim, H.S.,Lee, S.J.,Yoon, H.J.,An, D.R.,Kim, D.J.,Kim, S.J.,Suh, S.W.
Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases.
J.Struct.Biol., 175:442-450, 2011

PubMed Abstract: 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.

PubMed: 21605684
DOI: 10.1016/j.jsb.2011.05.007

Experimental method

X-RAY DIFFRACTION (1.8 Å)