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"
caption="1d7o, resolution 1.9&Aring;" />
'''CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN'''<br />


==Overview==
==CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN==
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.
<StructureSection load='1d7o' size='340' side='right'caption='[[1d7o]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d7o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brassica_napus Brassica napus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D7O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d7o OCA], [https://pdbe.org/1d7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d7o RCSB], [https://www.ebi.ac.uk/pdbsum/1d7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d7o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABI_BRANA FABI_BRANA] Catalyzes the NAD-dependent reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Catalyzes the last reduction step in the de novo synthesis cycle of fatty acids. Involved in the elongation cycle of fatty acids which are used in lipid metabolism. Required for normal plant growth (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d7/1d7o_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1d7o ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10610777 10610777]
[[Category: Brassica napus]]
[[Category: Brassica napus]]
[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Baker PJ]]
[[Category: Baker, P.J.]]
[[Category: Camble R]]
[[Category: Camble, R.]]
[[Category: Colls JG]]
[[Category: Colls, J.G.]]
[[Category: Levy C]]
[[Category: Levy, C.]]
[[Category: Minshull CA]]
[[Category: Minshull, C.A.]]
[[Category: Mistry A]]
[[Category: Mistry, A.]]
[[Category: Pauptit RA]]
[[Category: Pauptit, R.A.]]
[[Category: Rafferty JB]]
[[Category: Rafferty, J.B.]]
[[Category: Rice DW]]
[[Category: Rice, D.W.]]
[[Category: Roujeinikova A]]
[[Category: Roujeinikova, A.]]
[[Category: Rowsell S]]
[[Category: Rowsell, S.]]
[[Category: Sedelnikova S]]
[[Category: Sedelnikova, S.]]
[[Category: Slabas AR]]
[[Category: Slabas, A.R.]]
[[Category: Stuitje AR]]
[[Category: Stuitje, A.R.]]
[[Category: Viner R]]
[[Category: Viner, R]]
[[Category: NAD]]
[[Category: TCL]]
[[Category: enoyl reductase]]
[[Category: triclosan]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:04:20 2007''

Latest revision as of 09:50, 7 February 2024

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

Structural highlights

1d7o is a 1 chain structure with sequence from Brassica napus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABI_BRANA Catalyzes the NAD-dependent reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Catalyzes the last reduction step in the de novo synthesis cycle of fatty acids. Involved in the elongation cycle of fatty acids which are used in lipid metabolism. Required for normal plant growth (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1d7o, resolution 1.90Å

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