Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
Abstract

The molecular structure of the D-alanine:D-alanine ligase of the ddlB gene of Escherichia coli , co-crystallized with an S , R -methylphosphinate and adenosine triphosphate, was determined by x-ray diffraction to a resolution of 2.3 angstroms. A catalytic mechanism for the ligation of two D-alanine substrates is proposed in which a helix dipole and a hydrogen-bonded triad of tyrosine, serine, and glutamic acid assist binding and deprotonation steps. From sequence comparison, it is proposed that a different triad exists in a recently discovered D-alanine:D-lactate ligase (VanA) present in vancomycin-resistant enterococci. A molecular mechanism for the altered specificity of VanA is suggested.

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Fan, C., Moews, P. C., Walsh, C. T., & Knox, J. R. (1994). Vancomycin Resistance: Structure of D-Alanine:D-Alanine Ligase at 2.3 Å Resolution. Science, 266(5184), 439–443.

Authors 4
  1. Chang Fan (first)
  2. Paul C. Moews (additional)
  3. Christopher T. Walsh (additional)
  4. James R. Knox (additional)
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Dates
Type When
Created 18 years, 10 months ago (Oct. 5, 2006, 8:01 p.m.)
Deposited 1 year, 7 months ago (Jan. 14, 2024, 11:17 p.m.)
Indexed 1 month, 1 week ago (July 11, 2025, 9:05 p.m.)
Issued 30 years, 10 months ago (Oct. 21, 1994)
Published 30 years, 10 months ago (Oct. 21, 1994)
Published Print 30 years, 10 months ago (Oct. 21, 1994)
Funders 0

None

@article{Fan_1994, title={Vancomycin Resistance: Structure of D-Alanine:D-Alanine Ligase at 2.3 Å Resolution}, volume={266}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.7939684}, DOI={10.1126/science.7939684}, number={5184}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Fan, Chang and Moews, Paul C. and Walsh, Christopher T. and Knox, James R.}, year={1994}, month=oct, pages={439–443} }