%0 Journal Article %1 citeulike:677420 %A Lee, W. %A McDonough, M. A. %A Kotra, L. %A Li, Z. H. %A Silvaggi, N. R. %A Takeda, Y. %A Kelly, J. A. %A Mobashery, S. %C Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3125, USA. %D 2001 %J Proc Natl Acad Sci U S A %K k22 %N 4 %P 1427--1431 %R 10.1073/pnas.98.4.1427 %T A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis. %U http://dx.doi.org/10.1073/pnas.98.4.1427 %V 98 %X 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.

@article{citeulike:677420, abstract = {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.}, added-at = {2006-06-16T05:03:46.000+0200}, address = {Department of Molecular and Cell Biology, University of Connecticut, Storrs, CT 06269-3125, USA.}, author = {Lee, W. and McDonough, M. A. and Kotra, L. and Li, Z. H. and Silvaggi, N. R. and Takeda, Y. and Kelly, J. A. and Mobashery, S.}, biburl = {https://www.bibsonomy.org/bibtex/2c9e13b3d072430fbb6cbb8ce001ccd40/hlwoodcock}, citeulike-article-id = {677420}, doi = {10.1073/pnas.98.4.1427}, interhash = {177155c0ff0996a5076ccce25e9e930a}, intrahash = {c9e13b3d072430fbb6cbb8ce001ccd40}, issn = {0027-8424}, journal = {Proc Natl Acad Sci U S A}, keywords = {k22}, month = {February}, number = 4, pages = {1427--1431}, priority = {2}, timestamp = {2006-06-16T05:03:46.000+0200}, title = {A 1.2-A snapshot of the final step of bacterial cell wall biosynthesis.}, url = {http://dx.doi.org/10.1073/pnas.98.4.1427}, volume = 98, year = 2001 }