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1fqg
From Proteopedia
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| - | [[Image:1fqg.jpg|left|200px]] | + | [[Image:1fqg.jpg|left|200px]] |
| - | + | ||
| - | '''MOLECULAR STRUCTURE OF THE ACYL-ENZYME INTERMEDIATE IN TEM-1 BETA-LACTAMASE''' | + | {{Structure |
| + | |PDB= 1fqg |SIZE=350|CAPTION= <scene name='initialview01'>1fqg</scene>, resolution 1.7Å | ||
| + | |SITE= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MOLECULAR STRUCTURE OF THE ACYL-ENZYME INTERMEDIATE IN TEM-1 BETA-LACTAMASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1FQG is a [ | + | 1FQG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQG OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/1436034 1436034] |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| Line 18: | Line 27: | ||
[[Category: acyl-enzyme]] | [[Category: acyl-enzyme]] | ||
[[Category: beta-lactamase]] | [[Category: beta-lactamase]] | ||
| - | [[Category: class | + | [[Category: class some]] |
[[Category: penicillin]] | [[Category: penicillin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:12:38 2008'' |
Revision as of 09:12, 20 March 2008
| |||||||
| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| 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
Page seeded by OCA on Thu Mar 20 11:12:38 2008
