2enx

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spinqualitylabelsall models 2enx, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of the family II inorganic pyrophosphatase from Streptococcus agalactiae at 2.8 resolution

Overview

Streptococcus agalactiae, a prokaryote that causes infections in neonates, and immunocompromised adults, has a serine/threonine protein kinase (STK), signalling cascade. The structure of one of the targets, a family II, inorganic pyrophosphatase, has been solved by molecular replacement and, refined at 2.80 A resolution to an R factor of 19.2% (R(free) = 26.7%)., The two monomers in the asymmetric unit are related by a, noncrystallographic twofold axis, but the biological dimer is formed by a, crystallographic twofold. Each monomer contains the pyrophosphate analogue, imidodiphosphate (PNP) and three metal ions per active site: two Mn(2+), ions in sites M1 and M2 and an Mg(2+) ion in site M3. The enzyme is in the, closed conformation. Like other family II enzymes, the structure consists, of two domains (residues 1-191 and 198-311), with the active site located, between them. The conformation of Lys298 in the active site is different, from those observed previously and it coordinates to the conserved DHH, motif in a unique way. The structure suggests that Ser150, Ser194, Ser195, and Ser296 are the most likely targets for the Ser/Thr kinase and, phosphatase because they are surface-accessible and either in the active, site or in the hinge region between the two domains.

About this Structure

2ENX is a Single protein structure of sequence from Streptococcus agalactiae with MN, MG, 2PN and TRP as ligands. Active as Inorganic diphosphatase, with EC number 3.6.1.1 Full crystallographic information is available from OCA.

Reference

Structure of the Streptococcus agalactiae family II inorganic pyrophosphatase at 2.80 A resolution., Rantanen MK, Lehtio L, Rajagopal L, Rubens CE, Goldman A, Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):738-43. Epub 2007, May 15. PMID:17505113

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