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1iq6

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Revision as of 09:06, 17 January 2018

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

Structural highlights

1iq6 is a 2 chain structure with sequence from "aeromonas_caviae"_eddy_1962 "aeromonas caviae" eddy 1962. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:	Enoyl-CoA hydratase, with EC number 4.2.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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:12409309^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fukui T, Doi Y. Cloning and analysis of the poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) biosynthesis genes of Aeromonas caviae. J Bacteriol. 1997 Aug;179(15):4821-30. PMID:9244271
↑ Fukui T, Shiomi N, Doi Y. Expression and characterization of (R)-specific enoyl coenzyme A hydratase involved in polyhydroxyalkanoate biosynthesis by Aeromonas caviae. J Bacteriol. 1998 Feb;180(3):667-73. PMID:9457873
↑ Hisano T, Tsuge T, Fukui T, Iwata T, Miki K, Doi Y. Crystal structure of the (R)-specific enoyl-CoA hydratase from Aeromonas caviae involved in polyhydroxyalkanoate biosynthesis. J Biol Chem. 2003 Jan 3;278(1):617-24. Epub 2002 Oct 29. PMID:12409309 doi:10.1074/jbc.M205484200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1iq6"

@@ Line 1: / Line 1: @@
 ==(R)-HYDRATASE FROM A. CAVIAE INVOLVED IN PHA BIOSYNTHESIS==
 <StructureSection load='1iq6' size='340' side='right' caption='[[1iq6]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Enoyl-CoA_hydratase Enoyl-CoA hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.17 4.2.1.17] </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=1iq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iq6 OCA], [http://pdbe.org/1iq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1iq6 PDBsum]</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=1iq6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iq6 OCA], [http://pdbe.org/1iq6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1iq6 RCSB], [http://www.ebi.ac.uk/pdbsum/1iq6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1iq6 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 13: / Line 14: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iq/1iq6_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iq/1iq6_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1iq6" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Enoyl-CoA hydratase|Enoyl-CoA hydratase]]
 == References ==
 <references/>

1iq6

From Proteopedia

Revision as of 09:06, 17 January 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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