1fqg: Difference between revisions
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|PDB= 1fqg |SIZE=350|CAPTION= <scene name='initialview01'>1fqg</scene>, resolution 1.7Å | |PDB= 1fqg |SIZE=350|CAPTION= <scene name='initialview01'>1fqg</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=PNM:OPEN FORM - PENICILLIN G'>PNM</scene> | |LIGAND= <scene name='pdbligand=PNM:OPEN+FORM+-+PENICILLIN+G'>PNM</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1tem|1TEM]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqg OCA], [http://www.ebi.ac.uk/pdbsum/1fqg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fqg RCSB]</span> | |||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Strynadka, N C.]] | [[Category: Strynadka, N C.]] | ||
[[Category: acyl-enzyme]] | [[Category: acyl-enzyme]] | ||
[[Category: beta-lactamase]] | [[Category: beta-lactamase]] | ||
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[[Category: penicillin]] | [[Category: penicillin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:28:13 2008'' | ||
Revision as of 17:28, 30 March 2008
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| 1fqg, resolution 1.7Å | |||||||||||||
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| Ligands: | PNM | ||||||||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||||||||
| Related: | 1TEM
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
MOLECULAR STRUCTURE OF THE ACYL-ENZYME INTERMEDIATE IN TEM-1 BETA-LACTAMASE
Overview
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.
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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