|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
2001-2-26
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
The cell wall imparts structural strength and shape to bacteria. It is made up of polymeric glycan chains with peptide branches that are cross-linked to form the cell wall. The cross-linking reaction, catalyzed by transpeptidases, is the last step in cell wall biosynthesis. These enzymes are members of the family of penicillin-binding proteins, the targets of beta-lactam antibiotics. We report herein the structure of a penicillin-binding protein complexed with a cephalosporin designed to probe the mechanism of the cross-linking reaction catalyzed by transpeptidases. The 1.2-A resolution x-ray structure of this cephalosporin bound to the active site of the bifunctional serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase (EC ) from Streptomyces sp. strain R61 reveals how the two peptide strands from the polymeric substrates are sequestered in the active site of a transpeptidase. The structure of this complex provides a snapshot of the enzyme and the bound cell wall components poised for the final and critical cross-linking step of cell wall biosynthesis.
|
|
pubmed:grant |
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-11171944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-1436736,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-15299354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-1758883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-2025413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-4568761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-5219821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-7123246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-7626623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-8605631,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-9449253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-9614972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11171967-9757107
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0027-8424
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
13
|
|
pubmed:volume |
98
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1427-31
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:11171967-Acylation,
pubmed-meshheading:11171967-Carboxypeptidases,
pubmed-meshheading:11171967-Cell Wall,
pubmed-meshheading:11171967-Cephalosporins,
pubmed-meshheading:11171967-Computer Simulation,
pubmed-meshheading:11171967-Crystallography, X-Ray,
pubmed-meshheading:11171967-Models, Molecular,
pubmed-meshheading:11171967-Molecular Structure,
pubmed-meshheading:11171967-Protein Structure, Secondary,
pubmed-meshheading:11171967-Serine-Type D-Ala-D-Ala Carboxypeptidase,
pubmed-meshheading:11171967-Streptomyces
|
|
pubmed:year |
2001
|
|
pubmed:articleTitle |
A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis.
|
|
pubmed:affiliation |
Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3125, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|
