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PDBsum entry 3ga9
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Crystal structure of bacillus anthracis transpeptidase enzyme capd, crystal form ii
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Structure:
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Capsule biosynthesis protein capd. Chain: l. Fragment: unp residues 29-351. Engineered: yes. Other_details: large chain. Capsule biosynthesis protein capd. Chain: s. Fragment: unp residues 352-528. Engineered: yes.
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Source:
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Bacillus anthracis. Organism_taxid: 1392. Strain: a0389. Gene: bak_b0097, bxb0063, capd, dep, gbaa_pxo2_0063, pxo2-55. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: capd, dep, pxo2-55, bxb0063, gbaa_pxo2_0063.
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Resolution:
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2.30Å
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R-factor:
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0.200
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R-free:
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0.252
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Authors:
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R.Zhang,R.Wu,S.Richter,V.J.Anderson,D.Missiakas,A.Joachimiak
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Key ref:
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R.Wu
et al.
(2009).
Crystal structure of Bacillus anthracis transpeptidase enzyme CapD.
J Biol Chem,
284,
24406-24414.
PubMed id:
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Date:
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16-Feb-09
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Release date:
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16-Jun-09
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PROCHECK
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Headers
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References
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J Biol Chem
284:24406-24414
(2009)
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PubMed id:
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Crystal structure of Bacillus anthracis transpeptidase enzyme CapD.
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R.Wu,
S.Richter,
R.G.Zhang,
V.J.Anderson,
D.Missiakas,
A.Joachimiak.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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K.Wada,
M.Irie,
H.Suzuki,
and
K.Fukuyama
(2010).
Crystal structure of the halotolerant gamma-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals a unique architecture of the solvent-exposed catalytic pocket.
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FEBS J,
277,
1000-1009.
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PDB code:
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A.Fouet
(2009).
The surface of Bacillus anthracis.
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Mol Aspects Med,
30,
374-385.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
