2cla

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[[Image:2cla.jpg|left|200px]]
[[Image:2cla.jpg|left|200px]]
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{{Structure
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|PDB= 2cla |SIZE=350|CAPTION= <scene name='initialview01'>2cla</scene>, resolution 2.35&Aring;
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The line below this paragraph, containing "STRUCTURE_2cla", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CO:COBALT+(II)+ION'>CO</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/Chloramphenicol_O-acetyltransferase Chloramphenicol O-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.28 2.3.1.28] </span>
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{{STRUCTURE_2cla| PDB=2cla | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cla OCA], [http://www.ebi.ac.uk/pdbsum/2cla PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2cla RCSB]</span>
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'''CRYSTAL STRUCTURE OF THE ASP-199-ASN MUTANT OF CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF DISRUPTION OF A BURIED SALT-BRIDGE'''
'''CRYSTAL STRUCTURE OF THE ASP-199-ASN MUTANT OF CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF DISRUPTION OF A BURIED SALT-BRIDGE'''
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[[Category: Leslie, A G.W.]]
[[Category: Leslie, A G.W.]]
[[Category: Moody, P C.E.]]
[[Category: Moody, P C.E.]]
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[[Category: transferase (acyltransferase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:24:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:23:03 2008''
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Revision as of 19:24, 3 May 2008

Image:2cla.jpg

Template:STRUCTURE 2cla

CRYSTAL STRUCTURE OF THE ASP-199-ASN MUTANT OF CHLORAMPHENICOL ACETYLTRANSFERASE TO 2.35 ANGSTROMS RESOLUTION. STRUCTURAL CONSEQUENCES OF DISRUPTION OF A BURIED SALT-BRIDGE


Overview

The crystal structure of the Asp-199----Asn mutant of chloramphenicol acetyltransferase (CAT) has been determined to 2.35-A resolution. In wild-type CAT Asp-199 is involved in a fully buried intrasubunit salt bridge with Arg-18, an interaction that is adjacent to the active site. Replacement of aspartate with asparagine by site-directed mutagenesis disrupts this salt bridge and causes extensive conformational changes within the active site. The imidazole group of the catalytically essential His-195 is reoriented, with the loss of interactions thought to stabilize the preferred tautomer of this residue. Arg-18 and Asn-199 form three new intersubunit interactions as a result of large side-chain torsion angle changes which cause the movement of two polypeptide loops, some residues of which are up to 20 A away from the site of the mutation. The new interactions of Arg-18 and Asn-199 compensate for the loss of the buried salt bridge and afford near-wild-type thermostability to Asn-199 CAT, albeit with a greatly reduced activity.

About this Structure

2CLA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the aspartic acid-199----asparagine mutant of chloramphenicol acetyltransferase to 2.35-A resolution: structural consequences of disruption of a buried salt bridge., Gibbs MR, Moody PC, Leslie AG, Biochemistry. 1990 Dec 25;29(51):11261-5. PMID:2271709 Page seeded by OCA on Sat May 3 22:24:54 2008

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