期刊
JOURNAL OF MOLECULAR BIOLOGY
卷 388, 期 2, 页码 345-355出版社
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2009.03.040
关键词
DltA/ATP complex; AMP-forming domain; D-alanine activating enzyme; DltA; adenylation
资金
- Saskatchewan Health Research Foundation
- Canadian Institutes of Health Research Operating Grant [63860]
- Natural Sciences and Engineering Research Council of Canada
- National Research Council
- Canadian Institutes of Health Research
- University of Saskatchewan
D-Alanylation of lipoteichoic acids modulates the surface charge and ligand binding of the Gram-positive cell wall. Disruption of the bacterial dlt operon involved in teichoic acid alanylation, as well as inhibition of the DltA (D-alanyl carrier protein ligase) protein, has been shown to render the bacterium more susceptible to conventional antibiotics and host defense responses. The DltA catalyzes the adenylation and thiolation reactions of D-alanine. This enzyme belongs to a superfamily of AMP-forming domains such as the ubiquitous acetyl-coenzyme A synthetase. We have determined the 1.9-angstrom-resolution crystal structure of a DltA protein from Bacillus cereus in complex with ATP. This structure sheds light on the geometry of the bound ATP. The invariant catalytic residue Lys492 appears to be mobile, suggesting a molecular mechanism of catalysis for this superfamily of enzymes. Specific roles are also revealed for two other invariant residues: the divalent cation-stabilizing Glu298 and the beta-phosphate-interacting Arg397. Mutant proteins with a glutamine substitution at position 298 or 397 are inactive. (C) 2009 Elsevier Ltd. All rights reserved.
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