1d7o: Difference between revisions

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New page: left|200px<br /><applet load="1d7o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d7o, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1d7o.jpg|left|200px]]<br /><applet load="1d7o" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1d7o.jpg|left|200px]]<br /><applet load="1d7o" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1d7o, resolution 1.9&Aring;" />
caption="1d7o, resolution 1.9&Aring;" />
'''CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN'''<br />
'''CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN'''<br />


==Overview==
==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.
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==
==About this Structure==
1D7O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brassica_napus Brassica napus] with NAD and TCL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D7O OCA].  
1D7O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brassica_napus Brassica napus] with <scene name='pdbligand=NAD:'>NAD</scene> and <scene name='pdbligand=TCL:'>TCL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7O OCA].  


==Reference==
==Reference==
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[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Baker, P.J.]]
[[Category: Baker, P J.]]
[[Category: Camble, R.]]
[[Category: Camble, R.]]
[[Category: Colls, J.G.]]
[[Category: Colls, J G.]]
[[Category: Levy, C.]]
[[Category: Levy, C.]]
[[Category: Minshull, C.A.]]
[[Category: Minshull, C A.]]
[[Category: Mistry, A.]]
[[Category: Mistry, A.]]
[[Category: Pauptit, R.A.]]
[[Category: Pauptit, R A.]]
[[Category: Rafferty, J.B.]]
[[Category: Rafferty, J B.]]
[[Category: Rice, D.W.]]
[[Category: Rice, D W.]]
[[Category: Roujeinikova, A.]]
[[Category: Roujeinikova, A.]]
[[Category: Rowsell, S.]]
[[Category: Rowsell, S.]]
[[Category: Sedelnikova, S.]]
[[Category: Sedelnikova, S.]]
[[Category: Slabas, A.R.]]
[[Category: Slabas, A R.]]
[[Category: Stuitje, A.R.]]
[[Category: Stuitje, A R.]]
[[Category: Viner, R]]
[[Category: Viner, R]]
[[Category: NAD]]
[[Category: NAD]]
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[[Category: triclosan]]
[[Category: triclosan]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:04:20 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:55 2008''

Revision as of 13:13, 21 February 2008

File:1d7o.jpg


1d7o, resolution 1.9Å

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

OverviewOverview

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 StructureAbout this Structure

1D7O is a Single protein structure of sequence from Brassica napus with and as ligands. Active as [acyl-carrier-protein_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number 1.3.1.9 Full crystallographic information is available from OCA.

ReferenceReference

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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