3zu2

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[[Image:3zu2.png|left|200px]]
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==Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (SIRAS)==
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<StructureSection load='3zu2' size='340' side='right' caption='[[3zu2]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3zu2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZU2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZU2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3zu3|3zu3]], [[3zu4|3zu4]], [[3zu5|3zu5]]</td></tr>
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<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=3zu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zu2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zu2 RCSB], [http://www.ebi.ac.uk/pdbsum/3zu2 PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/Y4104_YERPE Y4104_YERPE]] Probable reductase (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The recently discovered FabV enoyl-ACP reductase, which catalyzes the last step of the bacterial fatty acid biosynthesis (FAS-II) pathway, is a promising but unexploited drug target against the reemerging pathogen Yersinia pestis. The structure of Y. pestis FabV in complex with its cofactor reveals that the enzyme features the common architecture of the short-chain dehydrogenase reductase superfamily, but contains additional structural elements that are mostly folded around the usually flexible substrate-binding loop, thereby stabilizing it in a very tight conformation that seals the active site. The structures of FabV in complex with NADH and two newly developed 2-pyridone inhibitors provide insights for the development of new lead compounds, and suggest a mechanism by which the substrate-binding loop opens to admit the inhibitor, a motion that could also be coupled to the interaction of FabV with the acyl-carrier protein substrate.
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Structure of the Yersinia pestis FabV enoyl-ACP reductase and its interaction with two 2-pyridone inhibitors.,Hirschbeck MW, Kuper J, Lu H, Liu N, Neckles C, Shah S, Wagner S, Sotriffer CA, Tonge PJ, Kisker C Structure. 2012 Jan 11;20(1):89-100. PMID:22244758<ref>PMID:22244758</ref>
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The line below this paragraph, containing "STRUCTURE_3zu2", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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-->
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{{STRUCTURE_3zu2| PDB=3zu2 | SCENE= }}
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===Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (SIRAS)===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_22244758}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 22244758 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_22244758}}
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==About this Structure==
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[[3zu2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZU2 OCA].
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==Reference==
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<ref group="xtra">PMID:022244758</ref><references group="xtra"/>
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[[Category: Yersinia pestis]]
[[Category: Yersinia pestis]]
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[[Category: Hirschbeck, M W.]]
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[[Category: Hirschbeck, M W]]
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[[Category: Kisker, C.]]
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[[Category: Kisker, C]]
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[[Category: Kuper, J.]]
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[[Category: Kuper, J]]
[[Category: Fatty acid biosynthesis ii]]
[[Category: Fatty acid biosynthesis ii]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Short-chain dehydrogenase reductase superfamily]]
[[Category: Short-chain dehydrogenase reductase superfamily]]

Revision as of 15:55, 25 December 2014

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH (SIRAS)

3zu2, resolution 2.10Å

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