1cef
From Proteopedia
(New page: 200px<br /> <applet load="1cef" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cef, resolution 2.04Å" /> '''CEFOTAXIME COMPLEXE...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1CEF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]] with CEF as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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=1CEF OCA]]. | + | 1CEF is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]] with CEF as [[http://en.wikipedia.org/wiki/ligand ligand]]. 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: ACT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CEF OCA]]. |
==Reference== | ==Reference== | ||
Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases., Kuzin AP, Liu H, Kelly JA, Knox JR, Biochemistry. 1995 Jul 25;34(29):9532-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7626623 7626623] | Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases., Kuzin AP, Liu H, Kelly JA, Knox JR, Biochemistry. 1995 Jul 25;34(29):9532-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7626623 7626623] | ||
| + | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
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[[Category: penicillin target]] | [[Category: penicillin target]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:38:59 2007'' |
Revision as of 11:34, 30 October 2007
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CEFOTAXIME COMPLEXED WITH THE STREPTOMYCES R61 DD-PEPTIDASE
Overview
Two clinically-important beta-lactam antibiotics, cephalothin and, cefotaxime, have been observed by X-ray crystallography bound to the, reactive Ser62 of the D-alanyl-D-alanine carboxypeptidase/transpeptidase, of Streptomyces sp. R61. Refinement of the two crystal structures produced, R factors for 3 sigma (F) data of 0.166 (to 1.8 A) and 0.170 (to 2.0 A), for the cephalothin and cefotaxime complexes, respectively. In each, complex, a water molecule is within 3.1 and 3.6 A of the acylated, beta-lactam carbonyl carbon atom, but is poorly activated by active site, residues for nucleophilic attack and deacylation. This apparent lack of, good stereochemistry for facile hydrolysis is in accord with the long, half-lives of cephalosporin intermediates in solution (20-40 h) and the, efficacy of ... [(full description)]
About this Structure
1CEF is a [Single protein] structure of sequence from [Streptomyces sp.] with CEF as [ligand]. Active as [Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [3.4.16.4]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
Binding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases., Kuzin AP, Liu H, Kelly JA, Knox JR, Biochemistry. 1995 Jul 25;34(29):9532-40. PMID:7626623
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