2ENX

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

Summary for 2ENX

• Entry DOI: 10.2210/pdb2enx/pdb
• Descriptor: Manganese-dependent inorganic pyrophosphatase, MANGANESE (II) ION, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: streptococcus agalactiae, family ii, inorganic, pyrophosphatase, signalling, phosphorylation, hydrolase
• Biological source: Streptococcus agalactiae
• Cellular location: Cytoplasm (By similarity): Q3K0B5
• Total number of polymer chains: 2
• Total formula weight: 68015.86

Authors

Rantanen, M.K.,Lehtio, L.,Rajagopal, L.,Rubens, C.E.,Goldman, A. (deposition date: 2007-03-28, release date: 2007-05-29, Last modification date: 2023-10-25)

Primary citation

Rantanen, M.K.,Lehtio, L.,Rajagopal, L.,Rubens, C.E.,Goldman, A.
Structure of the Streptococcus agalactiae family II inorganic pyrophosphatase at 2.80 A resolution
ACTA CRYSTALLOGR.,SECT.D, 63:738-743, 2007

PubMed Abstract: 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.

PubMed: 17505113
DOI: 10.1107/S0907444907019695

Experimental method

X-RAY DIFFRACTION (2.8 Å)