View source for 6hun


==Dimeric Archeal Rubisco from Hyperthermus butylicus==
<StructureSection load='6hun' size='340' side='right'caption='[[6hun]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hun]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyperthermus_butylicus_DSM_5456 Hyperthermus butylicus DSM 5456]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HUN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.802&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=6hun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hun OCA], [https://pdbe.org/6hun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hun RCSB], [https://www.ebi.ac.uk/pdbsum/6hun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hun ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2BK54_HYPBU A2BK54_HYPBU] Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.[HAMAP-Rule:MF_01133]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) from the hyperthermophilic archaeon Hyperthermus butylicus is presented at 1.8 A resolution. Previous structures of archaeal Rubisco have been found to assemble into decamers, and this oligomerization was thought to be required for a highly thermally stable enzyme. In the current study, H. butylicus Rubisco is shown to exist as a dimer in solution, yet has a thermal denaturation midpoint of 114 degrees C, suggesting that high thermal stability can be achieved without an increased oligomeric state. This increased thermal stability appears to be due to an increased number of electrostatic interactions within the monomeric subunit. As such, H. butylicus Rubisco presents a well characterized system in which to investigate the role of assembly and thermal stability in enzyme function.

Structure of a hyperthermostable dimeric archaeal Rubisco from Hyperthermus butylicus.,Bundela R, Keown J, Watkin S, Pearce FG Acta Crystallogr D Struct Biol. 2019 Jun 1;75(Pt 6):536-544. doi:, 10.1107/S2059798319006466. Epub 2019 May 28. PMID:31205016<ref>PMID:31205016</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6hun" style="background-color:#fffaf0;"></div>

==See Also==
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Hyperthermus butylicus DSM 5456]]
[[Category: Large Structures]]
[[Category: Bundela R]]
[[Category: Keown JR]]
[[Category: Pearce FG]]