5t6o: Difference between revisions
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<StructureSection load='5t6o' size='340' side='right' caption='[[5t6o]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5t6o' size='340' side='right' caption='[[5t6o]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5t6o]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T6O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T6O FirstGlance]. <br> | <table><tr><td colspan='2'>[[5t6o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17697_[[alcaligenes_eutrophus]] Atcc 17697 [[alcaligenes eutrophus]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T6O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T6O FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">phaC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=106590 ATCC 17697 [[Alcaligenes eutrophus]]])</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=5t6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t6o OCA], [http://pdbe.org/5t6o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t6o RCSB], [http://www.ebi.ac.uk/pdbsum/5t6o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t6o ProSAT]</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=5t6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t6o OCA], [http://pdbe.org/5t6o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t6o RCSB], [http://www.ebi.ac.uk/pdbsum/5t6o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t6o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Revision as of 17:21, 6 November 2017
Structure of the catalytic domain of the class I polyhydroxybutyrate synthase from Cupriavidus necatorStructure of the catalytic domain of the class I polyhydroxybutyrate synthase from Cupriavidus necator
Structural highlights
Publication Abstract from PubMedPolyhydroxybutyrate (PHB) synthase (PhaC) catalyzes the polymerization of 3-(R)-hydroxybutyryl-coenzyme A as a means of carbon storage in many bacteria. The resulting polymers can be used to make biodegradable materials with properties similar to those of thermoplastics and are an environmentally-friendly alternative to traditional petroleum-based plastics. A full biochemical and mechanistic understanding of this process has been hindered in part by a lack of structural information on PhaC. Here we present the first structure of the catalytic domain (residues 201-589) of the class I PhaC from Cupriavidus necator (formerly Ralstonia eutropha) to 1.80 A resolution. We observe a symmetrical dimeric architecture in which the active site of each monomer is separated from the other by ~33 A across an extensive dimer interface, suggesting a mechanism in which PHB biosynthesis occurs at a single active site. The structure additionally highlights key side chain interactions within the active site that play likely roles in facilitating catalysis, leading to the proposal of a modified mechanistic scheme involving two distinct roles for the active site histidine. We also identify putative substrate entrance and product egress routes within the enzyme, which are discussed in the context of previously reported biochemical observations. Our structure lays a foundation for further biochemical and structural characterization of PhaC, which could assist in engineering efforts for the production of eco-friendly materials. Structure of the Catalytic Domain of the Class I Polyhydroxybutyrate Synthase from Cupriavidus necator.,Wittenborn EC, Jost M, Wei Y, Stubbe J, Drennan CL J Biol Chem. 2016 Oct 14. pii: jbc.M116.756833. PMID:27742839[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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