3ga9

Crystal structure of Bacillus anthracis transpeptidase enzyme CapD, crystal form II

spinqualitylabelsall models 3ga9, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ga9 is a 2 chain structure with sequence from "bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLU NonStd Res: MSE Related: 3g9k Gene: BAK_B0097, BXB0063, capD, dep, GBAA_pXO2_0063, pXO2-55 ("Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946), capD, dep, pXO2-55, BXB0063, GBAA_pXO2_0063 ("Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CAPD_BACAN] Degradation of the high-molecular weight capsule (H-capsule) to the lower-molecular weight capsule (L-capsule), which is released from the bacterial cell surface. The production of L-capsule is essential to mediate escape from host defenses. Does not have gamma-glutamyltranspeptidase (GGT) activity. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Bacillus anthracis elaborates a poly-gamma-d-glutamic acid capsule that protects bacilli from phagocytic killing during infection. The enzyme CapD generates amide bonds with peptidoglycan cross-bridges to anchor capsular material within the cell wall envelope of B. anthracis. The capsular biosynthetic pathway is essential for virulence during anthrax infections and can be targeted for anti-infective inhibition with small molecules. Here, we present the crystal structures of the gamma-glutamyltranspeptidase CapD with and without alpha-l-Glu-l-Glu dipeptide, a non-hydrolyzable analog of poly-gamma-d-glutamic acid, in the active site. Purified CapD displays transpeptidation activity in vitro, and its structure reveals an active site broadly accessible for poly-gamma-glutamate binding and processing. Using structural and biochemical information, we derive a mechanistic model for CapD catalysis whereby Pro(427), Gly(428), and Gly(429) activate the catalytic residue of the enzyme, Thr(352), and stabilize an oxyanion hole via main chain amide hydrogen bonds. Crystal structure of Bacillus anthracis transpeptidase enzyme CapD.,Wu R, Richter S, Zhang RG, Anderson VJ, Missiakas D, Joachimiak A J Biol Chem. 2009 Sep 4;284(36):24406-14. Epub 2009 Jun 16. PMID:19535342 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA