3FCC

CRYSTAL STRUCTURE OF DLTA PROTEIN IN COMPLEX WITH ATP and MAGNESIUM

Summary for 3FCC

• Entry DOI: 10.2210/pdb3fcc/pdb
• Related: 3DHV 3FCE
• Descriptor: D-alanine--poly(phosphoribitol) ligase subunit 1, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: dlta, amp-forming domain, d-alanine, adenylation, d-alanine carrier protein ligase, atp complex, ligase
• Biological source: Bacillus cereus
• Cellular location: Cytoplasm (Probable): Q81G39
• Total number of polymer chains: 1
• Total formula weight: 58157.20

Authors

Osman, K.T.,Du, L.,He, Y.,Luo, Y. (deposition date: 2008-11-21, release date: 2009-04-14, Last modification date: 2023-09-06)

Primary citation

Osman, K.T.,Du, L.,He, Y.,Luo, Y.
Crystal structure of Bacillus cereus D-alanyl carrier protein ligase (DltA) in complex with ATP.
J.Mol.Biol., 388:345-355, 2009

PubMed Abstract: 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-A-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.

PubMed: 19324056
DOI: 10.1016/j.jmb.2009.03.040

Experimental method

X-RAY DIFFRACTION (2.32 Å)