1cef
From Proteopedia
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| - | [[Image:1cef.gif|left|200px]]<br /><applet load="1cef" size=" | + | [[Image:1cef.gif|left|200px]]<br /><applet load="1cef" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1cef, resolution 2.04Å" /> | caption="1cef, resolution 2.04Å" /> | ||
'''CEFOTAXIME COMPLEXED WITH THE STREPTOMYCES R61 DD-PEPTIDASE'''<br /> | '''CEFOTAXIME COMPLEXED WITH THE STREPTOMYCES R61 DD-PEPTIDASE'''<br /> | ||
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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/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] Known structural/functional Site: <scene name='pdbsite=ACT:Those For S. R61 Are Listed Below'>ACT</scene>. Full crystallographic information is available from [http:// | + | 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 <scene name='pdbligand=CEF:'>CEF</scene> 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] Known structural/functional Site: <scene name='pdbsite=ACT:Those+For+S.+R61+Are+Listed+Below'>ACT</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CEF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: penicillin target]] | [[Category: penicillin target]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:34:34 2008'' |
Revision as of 07:34, 3 February 2008
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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 these beta-lactams as inhibitors of bacterial cell wall, synthesis. Different hydrogen binding patterns of the two cephalosporins, to Thr301 are consistent with the low cefotaxime affinity of an altered, penicillin-binding protein, PBP-2x, reported in cefotaxime-resistant, strains of Streptococcus pneumoniae, and with the ability of mutant class, A beta-lactamases to hydrolyze third-generation cephalosporins.
About this Structure
1CEF is a Single protein structure of sequence from Streptomyces sp. with as ligand. Active as Serine-type D-Ala-D-Ala carboxypeptidase, with EC number 3.4.16.4 Known structural/functional Site: . 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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