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.
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| 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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Uchida I, Makino S, Sasakawa C, Yoshikawa M, Sugimoto C, Terakado N. Identification of a novel gene, dep, associated with depolymerization of the capsular polymer in Bacillus anthracis. Mol Microbiol. 1993 Aug;9(3):487-96. PMID:8105361
- ↑ Makino S, Watarai M, Cheun HI, Shirahata T, Uchida I. Effect of the lower molecular capsule released from the cell surface of Bacillus anthracis on the pathogenesis of anthrax. J Infect Dis. 2002 Jul 15;186(2):227-33. Epub 2002 Jun 27. PMID:12134259 doi:http://dx.doi.org/JID020035
- ↑ Wu R, Richter S, Zhang RG, Anderson VJ, Missiakas D, Joachimiak A. Crystal structure of Bacillus anthracis transpeptidase enzyme CapD. J Biol Chem. 2009 Sep 4;284(36):24406-14. Epub 2009 Jun 16. PMID:19535342 doi:10.1074/jbc.M109.019034
