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[[Image:1d7o.jpg|left|200px]]


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==CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN==
The line below this paragraph, containing "STRUCTURE_1d7o", creates the "Structure Box" on the page.
<StructureSection load='1d7o' size='340' side='right'caption='[[1d7o]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</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>
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<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>
{{STRUCTURE_1d7o| PDB=1d7o |  SCENE= }}
<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>


'''CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN'''
==See Also==
 
*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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 [http://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].
 
==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:[http://www.ncbi.nlm.nih.gov/pubmed/10610777 10610777]
[[Category: Brassica napus]]
[[Category: Brassica napus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Baker, P J.]]
[[Category: Baker PJ]]
[[Category: Camble, R.]]
[[Category: Camble R]]
[[Category: Colls, J G.]]
[[Category: Colls JG]]
[[Category: Levy, C.]]
[[Category: Levy C]]
[[Category: Minshull, C A.]]
[[Category: Minshull CA]]
[[Category: Mistry, A.]]
[[Category: Mistry A]]
[[Category: Pauptit, R A.]]
[[Category: Pauptit RA]]
[[Category: Rafferty, J B.]]
[[Category: Rafferty JB]]
[[Category: Rice, D W.]]
[[Category: Rice DW]]
[[Category: Roujeinikova, A.]]
[[Category: Roujeinikova A]]
[[Category: Rowsell, S.]]
[[Category: Rowsell S]]
[[Category: Sedelnikova, S.]]
[[Category: Sedelnikova S]]
[[Category: Slabas, A R.]]
[[Category: Slabas AR]]
[[Category: Stuitje, A R.]]
[[Category: Stuitje AR]]
[[Category: Viner, R]]
[[Category: Viner R]]
[[Category: Enoyl reductase]]
[[Category: Triclosan]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:32:22 2008''

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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