1hd8: Difference between revisions
New page: left|200px<br /> <applet load="1hd8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hd8, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF... |
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==About this Structure== | ==About this Structure== | ||
1HD8 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HD8 OCA]]. | 1HD8 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. Active as [[http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4]]. Structure known Active Site: S44. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HD8 OCA]]. | ||
==Reference== | ==Reference== | ||
Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution., Davies C, White SW, Nicholas RA, J Biol Chem. 2001 Jan 5;276(1):616-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10967102 10967102] | Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution., Davies C, White SW, Nicholas RA, J Biol Chem. 2001 Jan 5;276(1):616-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10967102 10967102] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Davies, C.]] | [[Category: Davies, C.]] | ||
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[[Category: peptidoglycan synthesis]] | [[Category: peptidoglycan synthesis]] | ||
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Revision as of 14:57, 30 October 2007
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CRYSTAL STRUCTURE OF A DEACYLATION-DEFECTIVE MUTANT OF PENICILLIN-BINDING PROTEIN 5 AT 2.3 A RESOLUTION
OverviewOverview
Penicillin-binding protein 5 (PBP 5) of Escherichia coli functions as a, d-alanine carboxypeptidase, cleaving the C-terminal d-alanine residue from, cell wall peptides. Like all PBPs, PBP 5 forms a covalent acyl-enzyme, complex with beta-lactam antibiotics; however, PBP 5 is distinguished by, its high rate of deacylation of the acyl-enzyme complex (t(12), approximately 9 min). A Gly-105 --> Asp mutation in PBP 5 markedly impairs, this beta-lactamase activity (deacylation), with only minor effects on, acylation, and promotes accumulation of a covalent complex with peptide, substrates. To gain further insight into the catalytic mechanism of PBP 5, we determined the three-dimensional structure of the G105D mutant form of, soluble PBP 5 (termed sPBP 5') at 2.3 A resolution. The structure ... [(full description)]
About this StructureAbout this Structure
1HD8 is a [Single protein] structure of sequence from [Escherichia coli]. Active as [Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [3.4.16.4]. Structure known Active Site: S44. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of a deacylation-defective mutant of penicillin-binding protein 5 at 2.3-A resolution., Davies C, White SW, Nicholas RA, J Biol Chem. 2001 Jan 5;276(1):616-23. PMID:10967102
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