1d7o

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|PDB= 1d7o |SIZE=350|CAPTION= <scene name='initialview01'>1d7o</scene>, resolution 1.9&Aring;
|PDB= 1d7o |SIZE=350|CAPTION= <scene name='initialview01'>1d7o</scene>, resolution 1.9&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene>
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|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=[[1eno|1ENO]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7o OCA], [http://www.ebi.ac.uk/pdbsum/1d7o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d7o RCSB]</span>
}}
}}
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[[Category: Stuitje, A R.]]
[[Category: Stuitje, A R.]]
[[Category: Viner, R]]
[[Category: Viner, R]]
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[[Category: NAD]]
 
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[[Category: TCL]]
 
[[Category: enoyl reductase]]
[[Category: enoyl reductase]]
[[Category: triclosan]]
[[Category: triclosan]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:34:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:36:28 2008''

Revision as of 16:36, 30 March 2008


PDB ID 1d7o

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: ,
Activity: [acyl-carrier-protein_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number 1.3.1.9
Related: 1ENO


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN


Overview

Molecular genetic studies with strains of Escherichia coli resistant to triclosan, an ingredient of many anti-bacterial household goods, have suggested that this compound works by acting as an inhibitor of enoyl reductase (ENR) and thereby blocking lipid biosynthesis. We present structural analyses correlated with inhibition data, on the complexes of E. coli and Brassica napus ENR with triclosan and NAD(+) which reveal how triclosan acts as a site-directed, picomolar inhibitor of the enzyme by mimicking its natural substrate. Elements of both the protein and the nucleotide cofactor play important roles in triclosan recognition, providing an explanation for the factors controlling its tight binding to the enzyme and for the emergence of triclosan resistance.

About this Structure

1D7O is a Single protein structure of sequence from Brassica napus. Full crystallographic information is available from OCA.

Reference

Crystallographic analysis of triclosan bound to enoyl reductase., Roujeinikova A, Levy CW, Rowsell S, Sedelnikova S, Baker PJ, Minshull CA, Mistry A, Colls JG, Camble R, Stuitje AR, Slabas AR, Rafferty JB, Pauptit RA, Viner R, Rice DW, J Mol Biol. 1999 Nov 26;294(2):527-35. PMID:10610777[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]

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