1c14: Difference between revisions

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[[Image:1c14.gif|left|200px]]
{{Seed}}
[[Image:1c14.png|left|200px]]


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{{STRUCTURE_1c14|  PDB=1c14  |  SCENE=  }}  
{{STRUCTURE_1c14|  PDB=1c14  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX'''
===CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX===




==Overview==
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The crystal structure of the Escherichia coli enoyl reductase-NAD+-triclosan complex has been determined at 2.5 A resolution. The Ile192-Ser198 loop is either disordered or in an open conformation in the previously reported structures of the enzyme. This loop adopts a closed conformation in our structure, forming van der Waals interactions with the inhibitor and hydrogen bonds with the bound NAD+ cofactor. The opening and closing of this flipping loop is likely an important factor in substrate or ligand recognition. The closed conformation of the loop appears to be a critical feature for the enhanced binding potency of triclosan, and a key component in future structure-based inhibitor design.
The line below this paragraph, {{ABSTRACT_PUBMED_10595560}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_10595560}}


==About this Structure==
==About this Structure==
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[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Triclosan]]
[[Category: Triclosan]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:12:17 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:03:48 2008''

Revision as of 17:03, 30 June 2008

File:1c14.png

Template:STRUCTURE 1c14

CRYSTAL STRUCTURE OF E COLI ENOYL REDUCTASE-NAD+-TRICLOSAN COMPLEX

Template:ABSTRACT PUBMED 10595560

About this Structure

1C14 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Molecular basis for triclosan activity involves a flipping loop in the active site., Qiu X, Janson CA, Court RI, Smyth MG, Payne DJ, Abdel-Meguid SS, Protein Sci. 1999 Nov;8(11):2529-32. PMID:10595560

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