1iq6

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[[Image:1iq6.gif|left|200px]]
 
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==(R)-HYDRATASE FROM A. CAVIAE INVOLVED IN PHA BIOSYNTHESIS==
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The line below this paragraph, containing "STRUCTURE_1iq6", creates the "Structure Box" on the page.
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<StructureSection load='1iq6' size='340' side='right'caption='[[1iq6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1iq6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeromonas_caviae Aeromonas caviae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IQ6 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.5&#8491;</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=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
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{{STRUCTURE_1iq6| PDB=1iq6 | SCENE= }}
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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=1iq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iq6 OCA], [https://pdbe.org/1iq6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iq6 RCSB], [https://www.ebi.ac.uk/pdbsum/1iq6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iq6 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHAJ_AERCA PHAJ_AERCA] Catalyzes the hydration of trans-2-enoyl-CoA with a chain-length of 4-6 carbon atoms, forming the corresponding (3R)-3-hydroxyacyl-CoA.<ref>PMID:9244271</ref> <ref>PMID:9457873</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iq/1iq6_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1iq6 ConSurf].
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<div style="clear:both"></div>
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'''(R)-HYDRATASE FROM A. CAVIAE INVOLVED IN PHA BIOSYNTHESIS'''
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==See Also==
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*[[Enoyl-CoA hydratase 3D structures|Enoyl-CoA hydratase 3D structures]]
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== References ==
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==Overview==
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<references/>
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The (R)-specific enoyl coenzyme A hydratase ((R)-hydratase) from Aeromonas caviae catalyzes the addition of a water molecule to trans-2-enoyl coenzyme A (CoA), with a chain-length of 4-6 carbons, to produce the corresponding (R)-3-hydroxyacyl-CoA. It forms a dimer of identical subunits with a molecular weight of about 14,000 and is involved in polyhydroxyalkanoate (PHA) biosynthesis. The crystal structure of the enzyme has been determined at 1.5-A resolution. The structure of the monomer consists of a five-stranded antiparallel beta-sheet and a central alpha-helix, folded into a so-called "hot dog" fold, with an overhanging segment. This overhang contains the conserved residues including the hydratase 2 motif residues. In dimeric form, two beta-sheets are associated to form an extended 10-stranded beta-sheet, and the overhangs obscure the putative active sites at the subunit interface. The active site is located deep within the substrate-binding tunnel, where Asp(31) and His(36) form a catalytic dyad. These residues are catalytically important as confirmed by site-directed mutagenesis and are possibly responsible for the activation of a water molecule and the protonation of a substrate molecule, respectively. Residues such as Leu(65) and Val(130) are situated at the bottom of the substrate-binding tunnel, defining the preference of the enzyme for the chain length of the substrate. These results provide target residues for protein engineering, which will enhance the significance of this enzyme in the production of novel PHA polymers. In addition, this study provides the first structural information of the (R)-hydratase family and may facilitate further functional studies for members of the family.
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__TOC__
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</StructureSection>
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==About this Structure==
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1IQ6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aeromonas_punctata Aeromonas punctata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQ6 OCA].
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==Reference==
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Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis., Hisano T, Tsuge T, Fukui T, Iwata T, Miki K, Doi Y, J Biol Chem. 2003 Jan 3;278(1):617-24. Epub 2002 Oct 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12409309 12409309]
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[[Category: Aeromonas punctata]]
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[[Category: Enoyl-CoA hydratase]]
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[[Category: Single protein]]
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[[Category: Doi, Y.]]
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[[Category: Fukui, T.]]
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[[Category: Hisano, T.]]
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[[Category: Iwata, T.]]
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[[Category: Tsuge, T.]]
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[[Category: Aeromonas caviae]]
[[Category: Aeromonas caviae]]
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[[Category: Enoyl-coa hydratase]]
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[[Category: Large Structures]]
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[[Category: Hydratase]]
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[[Category: Doi Y]]
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[[Category: Polyhydroxyalkanoate]]
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[[Category: Fukui T]]
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[[Category: The hydratase 2 motif]]
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[[Category: Hisano T]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:16:27 2008''
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[[Category: Iwata T]]
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[[Category: Tsuge T]]

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(R)-HYDRATASE FROM A. CAVIAE INVOLVED IN PHA BIOSYNTHESIS

PDB ID 1iq6

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