3GA9
Crystal structure of Bacillus anthracis transpeptidase enzyme CapD, crystal form II
Summary for 3GA9
| Entry DOI | 10.2210/pdb3ga9/pdb |
| Related | 3G9K |
| Descriptor | Capsule biosynthesis protein capD, GLUTAMIC ACID, ... (4 entities in total) |
| Functional Keywords | capd protein, bacillus anthracis, the great lakes regional center of excellence, glrce, capsule biogenesis/degradation, virulence, hydrolase |
| Biological source | Bacillus anthracis More |
| Total number of polymer chains | 2 |
| Total formula weight | 56112.28 |
| Authors | Zhang, R.,Wu, R.,Richter, S.,Anderson, V.J.,Missiakas, D.,Joachimiak, A. (deposition date: 2009-02-16, release date: 2009-06-16, Last modification date: 2018-01-24) |
| Primary citation | Wu, R.,Richter, S.,Zhang, R.G.,Anderson, V.J.,Missiakas, D.,Joachimiak, A. Crystal Structure of Bacillus anthracis Transpeptidase Enzyme CapD. J.Biol.Chem., 284:24406-24414, 2009 Cited by PubMed Abstract: 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. PubMed: 19535342DOI: 10.1074/jbc.M109.019034 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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