1bvr: Difference between revisions

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-[[Image:1bvr.gif|left|200px]]
- {{Structure
+==M.TB. ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH NAD+ AND C16-FATTY-ACYL-SUBSTRATE==
-|PDB= 1bvr |SIZE=350|CAPTION= <scene name='initialview01'>1bvr</scene>, resolution 2.8&Aring;
+<StructureSection load='1bvr' size='340' side='right'caption='[[1bvr]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=THT:TRANS-2-HEXADECENOYL-(N-ACETYL-CYSTEAMINE)-THIOESTER'>THT</scene>
+<table><tr><td colspan='2'>[[1bvr]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BVR FirstGlance]. <br>
-|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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-|GENE=
+<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=THT:TRANS-2-HEXADECENOYL-(N-ACETYL-CYSTEAMINE)-THIOESTER'>THT</scene></td></tr>
-|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG0623 FabI], [http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=PRK07889 PRK07889]</span>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvr OCA], [https://pdbe.org/1bvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bvr RCSB], [https://www.ebi.ac.uk/pdbsum/1bvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bvr ProSAT], [https://www.topsan.org/Proteins/TBSGC/1bvr TOPSAN]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvr OCA], [http://www.ebi.ac.uk/pdbsum/1bvr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bvr RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/INHA_MYCTU INHA_MYCTU]
+== 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/bv/1bvr_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=1bvr ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Enoyl-ACP reductases participate in fatty acid biosynthesis by utilizing NADH to reduce the trans double bond between positions C2 and C3 of a fatty acyl chain linked to the acyl carrier protein. The enoyl-ACP reductase from Mycobacterium tuberculosis, known as InhA, is a member of an unusual FAS-II system that prefers longer chain fatty acyl substrates for the purpose of synthesizing mycolic acids, a major component of mycobacterial cell walls. The crystal structure of InhA in complex with NAD+ and a C16 fatty acyl substrate, trans-2-hexadecenoyl-(N-acetylcysteamine)-thioester, reveals that the substrate binds in a general "U-shaped" conformation, with the trans double bond positioned directly adjacent to the nicotinamide ring of NAD+. The side chain of Tyr158 directly interacts with the thioester carbonyl oxygen of the C16 fatty acyl substrate and therefore could help stabilize the enolate intermediate, proposed to form during substrate catalysis. Hydrophobic residues, primarily from the substrate binding loop (residues 196-219), engulf the fatty acyl chain portion of the substrate. The substrate binding loop of InhA is longer than that of other enoyl-ACP reductases and creates a deeper substrate binding crevice, consistent with the ability of InhA to recognize longer chain fatty acyl substrates.
-'''M.TB. ENOYL-ACP REDUCTASE (INHA) IN COMPLEX WITH NAD+ AND C16-FATTY-ACYL-SUBSTRATE'''
+Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate.,Rozwarski DA, Vilcheze C, Sugantino M, Bittman R, Sacchettini JC J Biol Chem. 1999 May 28;274(22):15582-9. PMID:10336454<ref>PMID:10336454</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1bvr" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Enoyl-ACP reductases participate in fatty acid biosynthesis by utilizing NADH to reduce the trans double bond between positions C2 and C3 of a fatty acyl chain linked to the acyl carrier protein. The enoyl-ACP reductase from Mycobacterium tuberculosis, known as InhA, is a member of an unusual FAS-II system that prefers longer chain fatty acyl substrates for the purpose of synthesizing mycolic acids, a major component of mycobacterial cell walls. The crystal structure of InhA in complex with NAD+ and a C16 fatty acyl substrate, trans-2-hexadecenoyl-(N-acetylcysteamine)-thioester, reveals that the substrate binds in a general "U-shaped" conformation, with the trans double bond positioned directly adjacent to the nicotinamide ring of NAD+. The side chain of Tyr158 directly interacts with the thioester carbonyl oxygen of the C16 fatty acyl substrate and therefore could help stabilize the enolate intermediate, proposed to form during substrate catalysis. Hydrophobic residues, primarily from the substrate binding loop (residues 196-219), engulf the fatty acyl chain portion of the substrate. The substrate binding loop of InhA is longer than that of other enoyl-ACP reductases and creates a deeper substrate binding crevice, consistent with the ability of InhA to recognize longer chain fatty acyl substrates.
+*[[Enoyl-Acyl-Carrier Protein Reductase 3D structures|Enoyl-Acyl-Carrier Protein Reductase 3D structures]]
+*[[Mannose-binding protein|Mannose-binding protein]]
-==About this Structure==
+== References ==
-BVR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVR OCA].
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate., Rozwarski DA, Vilcheze C, Sugantino M, Bittman R, Sacchettini JC, J Biol Chem. 1999 May 28;274(22):15582-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10336454 10336454]
+[[Category: Large Structures]]
-[[Category: Enoyl-[acyl-carrier-protein] reductase (NADH)]]
 [[Category: Mycobacterium tuberculosis]]
-[[Category: Single protein]]
+[[Category: Bittman R]]
-[[Category: Bittman, R.]]
+[[Category: Jacobs W]]
-[[Category: Jacobs, W.]]
+[[Category: Rozwarski DA]]
-[[Category: Rozwarski, D A.]]
+[[Category: Sugantino M]]
-[[Category: Sugantino, M.]]
+[[Category: Vilcheze C]]
-[[Category: TBSGC, TB Structural Genomics Consortium.]]
-[[Category: Vilcheze, C.]]
-[[Category: nadh-dependent enoyl-acp reductase]]
-[[Category: protein structure initiative]]
-[[Category: psi]]
-[[Category: structural genomic]]
-[[Category: tb structural genomics consortium]]
-[[Category: tbsgc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:09:17 2008''