3s46 | pdb_00003s46

The crystal structure of alanine racemase from streptococcus pneumoniae

spinqualitylabelsall models 3s46, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3s46 is a 2 chain structure with sequence from "diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886. This structure supersedes the now removed PDB entry 3mub. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BEZ NonStd Res: KCX, LLP Gene: alaR, alr, SP_1698 ("Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886) Activity: Alanine racemase, with EC number 5.1.1.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [ALR_STRPN] Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids (By similarity). Publication Abstract from PubMed ABSTRACT: BACKGROUND: Streptococcus pneumoniae is a globally important pathogen. The Gram-positive diplococcus is a leading cause of pneumonia, otitis media, bacteremia, and meningitis, and antibiotic resistant strains have become increasingly common over recent years. Alanine racemase is a ubiquitous enzyme among bacteria and provides the essential cell wall precursor, D-alanine. Since it is absent in humans, this enzyme is an attractive target for the development of drugs against S. pneumoniae and other bacterial pathogens. RESULTS: Here we report the crystal structure of alanine racemase from S. pneumoniae (AlrSP). Crystals diffracted to a resolution of 2.0 A and belong to the space group P3121 with the unit cell parameters a=b=119.97 A, c=118.10 A, alpha=beta=90degrees and gamma=120degrees. Structural comparisons show that AlrSP shares both an overall fold and key active site residues with other bacterial alanine racemases. The active site cavity is similar to other Gram positive alanine racemases, featuring a restricted but conserved entryway. CONCLUSIONS: We have solved the structure of AlrSP, an essential step towards the development of an accurate pharmacophore model of the enzyme, and an important contribution towards our on-going alanine racemase structure-based drug design project. We have identified three regions on the enzyme that could be targeted for inhibitor design, the active site, the dimer interface, and the active site entryway. The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design.,Im H, Sharpe ML, Strych U, Davlieva M, Krause KL BMC Microbiol. 2011 May 25;11(1):116. PMID:21612658 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alanine racemase

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