1ceg: Difference between revisions
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[[Image:1ceg.gif|left|200px]]<br /> | [[Image:1ceg.gif|left|200px]]<br /><applet load="1ceg" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1ceg" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1ceg, resolution 1.80Å" /> | caption="1ceg, resolution 1.80Å" /> | ||
'''CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE'''<br /> | '''CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1CEG 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 CEP 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] | 1CEG 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 CEP 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CEG OCA]. | ||
==Reference== | ==Reference== | ||
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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 Dec 18 14:37:44 2007'' | ||
Revision as of 15:27, 18 December 2007
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CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE
OverviewOverview
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 StructureAbout this Structure
1CEG is a Single protein structure of sequence from Streptomyces sp. with CEP 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.
ReferenceReference
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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