1fqg

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[[Image:1fqg.jpg|left|200px]]
[[Image:1fqg.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1fqg |SIZE=350|CAPTION= <scene name='initialview01'>1fqg</scene>, resolution 1.7&Aring;
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The line below this paragraph, containing "STRUCTURE_1fqg", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=PNM:OPEN+FORM+-+PENICILLIN+G'>PNM</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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-->
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|DOMAIN=
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{{STRUCTURE_1fqg| PDB=1fqg | SCENE= }}
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|RELATEDENTRY=[[1tem|1TEM]]
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|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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}}
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'''MOLECULAR STRUCTURE OF THE ACYL-ENZYME INTERMEDIATE IN TEM-1 BETA-LACTAMASE'''
'''MOLECULAR STRUCTURE OF THE ACYL-ENZYME INTERMEDIATE IN TEM-1 BETA-LACTAMASE'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Strynadka, N C.]]
[[Category: Strynadka, N C.]]
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[[Category: acyl-enzyme]]
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[[Category: Acyl-enzyme]]
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[[Category: beta-lactamase]]
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[[Category: Beta-lactamase]]
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[[Category: class some]]
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[[Category: Class some]]
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[[Category: penicillin]]
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[[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 Sun Mar 30 20:28:13 2008''
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Revision as of 13:38, 2 May 2008

Image:1fqg.jpg

Template:STRUCTURE 1fqg

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 Fri May 2 16:38:44 2008

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