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==CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN== | ==CRYSTAL STRUCTURE OF BRASSICA NAPUS ENOYL ACYL CARRIER PROTEIN REDUCTASE COMPLEXED WITH NAD AND TRICLOSAN== | ||
<StructureSection load='1d7o' size='340' side='right' caption='[[1d7o]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1d7o' size='340' side='right'caption='[[1d7o]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1d7o]] is a 1 chain structure with sequence from [ | <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><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <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> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </table> | ||
<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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d7/1d7o_consurf.spt"</scriptWhenChecked> | <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> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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> | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Enoyl-Acyl-Carrier Protein Reductase|Enoyl-Acyl-Carrier Protein Reductase]] | *[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Brassica napus]] | [[Category: Brassica napus]] | ||
[[Category: Baker | [[Category: Large Structures]] | ||
[[Category: Camble | [[Category: Baker PJ]] | ||
[[Category: Colls | [[Category: Camble R]] | ||
[[Category: Levy | [[Category: Colls JG]] | ||
[[Category: Minshull | [[Category: Levy C]] | ||
[[Category: Mistry | [[Category: Minshull CA]] | ||
[[Category: Pauptit | [[Category: Mistry A]] | ||
[[Category: Rafferty | [[Category: Pauptit RA]] | ||
[[Category: Rice | [[Category: Rafferty JB]] | ||
[[Category: Roujeinikova | [[Category: Rice DW]] | ||
[[Category: Rowsell | [[Category: Roujeinikova A]] | ||
[[Category: Sedelnikova | [[Category: Rowsell S]] | ||
[[Category: Slabas | [[Category: Sedelnikova S]] | ||
[[Category: Stuitje | [[Category: Slabas AR]] | ||
[[Category: Viner | [[Category: Stuitje AR]] | ||
[[Category: Viner R]] | |||
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
FunctionFABI_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 |
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