1fqg

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[[Image:1fqg.jpg|left|200px]]
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{{STRUCTURE_1fqg| PDB=1fqg | SCENE= }}
{{STRUCTURE_1fqg| PDB=1fqg | SCENE= }}
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'''MOLECULAR STRUCTURE OF THE ACYL-ENZYME INTERMEDIATE IN TEM-1 BETA-LACTAMASE'''
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===MOLECULAR STRUCTURE OF THE ACYL-ENZYME INTERMEDIATE IN TEM-1 BETA-LACTAMASE===
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==Overview==
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The X-ray crystal structure of the molecular complex of penicillin G with a deacylation-defective mutant of the RTEM-1 beta-lactamase from Escherichia coli shows how these antibiotics are recognized and destroyed. Penicillin G is covalently bound to Ser 70 0 gamma as an acyl-enzyme intermediate. The deduced catalytic mechanism uses Ser 70 0 gamma as the attacking nucleophile during acylation. Lys 73 N zeta acts as a general base in abstracting a proton from Ser 70 and transferring it to the thiazolidine ring nitrogen atom via Ser 130 0 gamma. Deacylation is accomplished by nucleophilic attack on the penicilloyl carbonyl carbon by a water molecule assisted by the general base, Glu 166.
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The line below this paragraph, {{ABSTRACT_PUBMED_1436034}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 1436034 is the PubMed ID number.
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{{ABSTRACT_PUBMED_1436034}}
==About this Structure==
==About this Structure==
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[[Category: Class some]]
[[Category: Class some]]
[[Category: Penicillin]]
[[Category: Penicillin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:38:44 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:47:10 2008''

Revision as of 00:47, 1 July 2008

Template:STRUCTURE 1fqg

MOLECULAR STRUCTURE OF THE ACYL-ENZYME INTERMEDIATE IN TEM-1 BETA-LACTAMASE

Template:ABSTRACT PUBMED 1436034

About this Structure

1FQG is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Molecular structure of the acyl-enzyme intermediate in beta-lactam hydrolysis at 1.7 A resolution., Strynadka NC, Adachi H, Jensen SE, Johns K, Sielecki A, Betzel C, Sutoh K, James MN, Nature. 1992 Oct 22;359(6397):700-5. PMID:1436034

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