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==Crystal structure of Bacillus subtilis beta-ketoacyl-ACP synthase II (FabF) in a covalent complex with cerulenin==
==Crystal structure of Bacillus subtilis beta-ketoacyl-ACP synthase II (FabF) in a covalent complex with cerulenin==
<StructureSection load='4ls8' size='340' side='right' caption='[[4ls8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='4ls8' size='340' side='right'caption='[[4ls8]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ls8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacsu Bacsu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LS8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LS8 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ls8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LS8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LS8 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1XG:(3R,7E,10E)-3-HYDROXY-4-OXODODECA-7,10-DIENAMIDE'>1XG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene><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]] 2.1&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ls5|4ls5]], [[4ls6|4ls6]], [[4ls7|4ls7]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1XG:(3R,7E,10E)-3-HYDROXY-4-OXODODECA-7,10-DIENAMIDE'>1XG</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabF, yjaY, BSU11340 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224308 BACSU])</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=4ls8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ls8 OCA], [https://pdbe.org/4ls8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ls8 RCSB], [https://www.ebi.ac.uk/pdbsum/4ls8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ls8 ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_II Beta-ketoacyl-[acyl-carrier-protein] synthase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.179 2.3.1.179] </span></td></tr>
</table>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ls8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ls8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ls8 RCSB], [http://www.ebi.ac.uk/pdbsum/4ls8 PDBsum]</span></td></tr>
== Function ==
<table>
[https://www.uniprot.org/uniprot/FABF_BACSU FABF_BACSU] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Structural insights into bacterial resistance to cerulenin.,Trajtenberg F, Altabe S, Larrieux N, Ficarra F, de Mendoza D, Buschiazzo A, Schujman GE FEBS J. 2014 Mar 19. doi: 10.1111/febs.12785. PMID:24641521<ref>PMID:24641521</ref>
Structural insights into bacterial resistance to cerulenin.,Trajtenberg F, Altabe S, Larrieux N, Ficarra F, de Mendoza D, Buschiazzo A, Schujman GE FEBS J. 2014 Mar 19. doi: 10.1111/febs.12785. PMID:24641521<ref>PMID:24641521</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4ls8" style="background-color:#fffaf0;"></div>
==See Also==
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacsu]]
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Buschiazzo, A.]]
[[Category: Large Structures]]
[[Category: Larrieux, N.]]
[[Category: Buschiazzo A]]
[[Category: Trajtenberg, F.]]
[[Category: Larrieux N]]
[[Category: Cerulenin]]
[[Category: Trajtenberg F]]
[[Category: Condensing enzyme]]
[[Category: Drug target]]
[[Category: Fatty acid elongation]]
[[Category: Kasii]]
[[Category: Ketoacyl synthase]]
[[Category: Transferase]]

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