4ia6

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==Hydratase from lactobacillus acidophilus in a ligand bound form (LA LAH)==
==Hydratase from lactobacillus acidophilus in a ligand bound form (LA LAH)==
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<StructureSection load='4ia6' size='340' side='right' caption='[[4ia6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='4ia6' size='340' side='right'caption='[[4ia6]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ia6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lacac Lacac]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IA6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IA6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ia6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_acidophilus_NCFM Lactobacillus acidophilus NCFM]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IA6 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=EIC:LINOLEIC+ACID'>EIC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ia5|4ia5]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EIC:LINOLEIC+ACID'>EIC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LBA0649 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272621 LACAC])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ia6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ia6 OCA], [https://pdbe.org/4ia6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ia6 RCSB], [https://www.ebi.ac.uk/pdbsum/4ia6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ia6 ProSAT]</span></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=4ia6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ia6 OCA], [http://pdbe.org/4ia6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ia6 RCSB], [http://www.ebi.ac.uk/pdbsum/4ia6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ia6 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q5FL96_LACAC Q5FL96_LACAC]
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Bacteria have evolved mechanisms for the hydrogenation of unsaturated fatty acids. Hydroxy fatty acid formation may be the first step in such a process; however, knowledge of the structural and mechanistic aspects of this reaction is scarce. Recently, myosin cross-reactive antigen was shown to be a bacterial FAD-containing hydratase which acts on the 9Z and 12Z double bonds of C16 and C18 non-esterified fatty acids, with the formation of 10-hydroxy and 10,13-dihydroxy fatty acids. These fatty acid hydratases form a large protein family which is conserved across Gram-positive and Gram-negative bacteria with no sequence similarity to any known protein apart from the FAD-binding motif. In order to shed light on the substrate recognition and the mechanism of the hydratase reaction, the crystal structure of the hydratase from Lactobacillus acidophilus (LAH) was determined by single-wavelength anomalous dispersion. Crystal structures of apo LAH and of LAH with bound linoleic acid were refined at resolutions of 2.3 and 1.8 A, respectively. LAH is a homodimer; each protomer consists of four intricately connected domains. Three of them form the FAD-binding and substrate-binding sites and reveal structural similarity to three domains of several flavin-dependent enzymes, including amine oxidoreductases. The additional fourth domain of LAH is located at the C-terminus and consists of three alpha-helices. It covers the entrance to the hydrophobic substrate channel leading from the protein surface to the active site. In the presence of linoleic acid, the fourth domain of one protomer undergoes conformational changes and opens the entrance to the substrate-binding channel of the other protomer of the LAH homodimer. The linoleic acid molecule is bound at the entrance to the substrate channel, suggesting movement of the lid domain triggered by substrate recognition.
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Crystal structure analysis of a fatty acid double-bond hydratase from Lactobacillus acidophilus.,Volkov A, Khoshnevis S, Neumann P, Herrfurth C, Wohlwend D, Ficner R, Feussner I Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):648-57. doi:, 10.1107/S0907444913000991. Epub 2013 Mar 14. PMID:23519674<ref>PMID:23519674</ref>
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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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<div class="pdbe-citations 4ia6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Lacac]]
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[[Category: Lactobacillus acidophilus NCFM]]
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[[Category: Ficner, R]]
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[[Category: Large Structures]]
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[[Category: Khoshnevis, S]]
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[[Category: Ficner R]]
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[[Category: Neumann, P]]
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[[Category: Khoshnevis S]]
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[[Category: Cla]]
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[[Category: Neumann P]]
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[[Category: Conjugated linoleic acid]]
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[[Category: Fad binding]]
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[[Category: Fatty acid]]
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[[Category: Hydratase]]
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[[Category: Immune system]]
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[[Category: Mcra]]
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[[Category: Rossmann fold]]
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Current revision

Hydratase from lactobacillus acidophilus in a ligand bound form (LA LAH)

PDB ID 4ia6

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