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==Crystal Structure of the Bacillus cereus Enoyl-Acyl Carrier Protein Reductase (Apo form)==
==Crystal Structure of the Bacillus cereus Enoyl-Acyl Carrier Protein Reductase (Apo form)==
<StructureSection load='3oje' size='340' side='right' caption='[[3oje]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
<StructureSection load='3oje' size='340' side='right'caption='[[3oje]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3oje]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baccr Baccr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OJE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OJE FirstGlance]. <br>
<table><tr><td colspan='2'>[[3oje]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OJE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OJE FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ojf|3ojf]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.02&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BC_1216 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=226900 BACCR])</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=3oje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oje OCA], [https://pdbe.org/3oje PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oje RCSB], [https://www.ebi.ac.uk/pdbsum/3oje PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oje ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3oje FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oje OCA], [http://pdbe.org/3oje PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3oje RCSB], [http://www.ebi.ac.uk/pdbsum/3oje PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3oje ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FABI_BACCR FABI_BACCR]] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).  
[https://www.uniprot.org/uniprot/FABI_BACCR FABI_BACCR] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (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/oj/3oje_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oj/3oje_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>
Line 21: Line 19:
</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=3oje ConSurf].
</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=3oje ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Enoyl-[acyl carrier protein] reductase (ENR) is an essential enzyme in type II fatty-acid synthesis that catalyzes the last step in each elongation cycle. Thus far FabI, FabL and FabK have been reported to carry out the reaction, with FabI being the most characterized. Some bacteria have more than one ENR, and Bacillus cereus has two (FabI and FabL) reported. Here, we have determined the crystal structures of the later in the apo form and in the ternary complex with NADP(+) and an indole naphthyridinone inhibitor. The two structures are almost identical, except for the three stretches that are disordered in the apo form. The apo form exists as a homo-dimer in both crystal and solution, while the ternary complex forms a homo-tetramer. The three stretches disordered in the apo structure are important in the cofactor and the inhibitor binding as well as in tetramer formation.
Dimeric and tetrameric forms of enoyl-acyl carrier protein reductase from Bacillus cereus.,Kim SJ, Ha BH, Kim KH, Hong SK, Shin KJ, Suh SW, Kim EE Biochem Biophys Res Commun. 2010 Oct 1;400(4):517-22. Epub 2010 Aug 26. PMID:20800575<ref>PMID:20800575</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3oje" style="background-color:#fffaf0;"></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]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Baccr]]
[[Category: Bacillus cereus ATCC 14579]]
[[Category: Ha, B H]]
[[Category: Large Structures]]
[[Category: Hong, S K]]
[[Category: Ha BH]]
[[Category: Kim, E E]]
[[Category: Hong SK]]
[[Category: Kim, K H]]
[[Category: Kim EE]]
[[Category: Kim, S J]]
[[Category: Kim KH]]
[[Category: Suh, S W]]
[[Category: Kim SJ]]
[[Category: Apo form]]
[[Category: Suh SW]]
[[Category: Enoyl-acp reductase]]
[[Category: Nad binding]]
[[Category: Oxidoreductase]]
[[Category: Rossmann fold]]

Latest revision as of 08:33, 20 March 2024

Crystal Structure of the Bacillus cereus Enoyl-Acyl Carrier Protein Reductase (Apo form)

3oje, resolution 3.02Å

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