5t6o: Difference between revisions

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==Structure of the catalytic domain of the class I polyhydroxybutyrate synthase from Cupriavidus necator==
==Structure of the catalytic domain of the class I polyhydroxybutyrate synthase from Cupriavidus necator==
<StructureSection load='5t6o' size='340' side='right' caption='[[5t6o]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='5t6o' size='340' side='right'caption='[[5t6o]], [[Resolution|resolution]] 1.80&Aring;' 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 [https://en.wikipedia.org/wiki/Cupriavidus_necator Cupriavidus necator]. 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 [https://proteopedia.org/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='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>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t6o OCA], [https://pdbe.org/5t6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t6o RCSB], [https://www.ebi.ac.uk/pdbsum/5t6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t6o ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/PHAC_CUPNH PHAC_CUPNH] Polymerizes (R)-3-hydroxybutyryl-CoA to create polyhydroxybutyrate (PHB) which consists of thousands of hydroxybutyrate molecules linked end to end. PHB serves as an intracellular energy reserve material when cells grow under conditions of nutrient limitation.<ref>PMID:2670936</ref>
Polyhydroxybutyrate (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<ref>PMID:27742839</ref>
==See Also==
 
*[[Polyhydroxybutyrate synthase|Polyhydroxybutyrate synthase]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5t6o" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Drennan, C L]]
[[Category: Cupriavidus necator]]
[[Category: Jost, M]]
[[Category: Large Structures]]
[[Category: Wittenborn, E C]]
[[Category: Drennan CL]]
[[Category: Alpha/beta hydrolase fold]]
[[Category: Jost M]]
[[Category: Biosynthetic protein]]
[[Category: Wittenborn EC]]
[[Category: Nontemplate-dependent polymerization]]
[[Category: Phac]]
[[Category: Polyhydroxybutyrate synthase]]
[[Category: Transferase]]

Latest revision as of 18:37, 6 March 2024

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

5t6o is a 1 chain structure with sequence from Cupriavidus necator. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PHAC_CUPNH Polymerizes (R)-3-hydroxybutyryl-CoA to create polyhydroxybutyrate (PHB) which consists of thousands of hydroxybutyrate molecules linked end to end. PHB serves as an intracellular energy reserve material when cells grow under conditions of nutrient limitation.[1]

See Also

References

  1. ↑ Peoples OP, Sinskey AJ. Poly-beta-hydroxybutyrate (PHB) biosynthesis in Alcaligenes eutrophus H16. Identification and characterization of the PHB polymerase gene (phbC). J Biol Chem. 1989 Sep 15;264(26):15298-303. PMID:2670936

5t6o, resolution 1.80Å

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