8tfo
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of MKvar== | |
| + | <StructureSection load='8tfo' size='340' side='right'caption='[[8tfo]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8tfo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ramazzottius_varieornatus Ramazzottius varieornatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8TFO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8TFO 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]] 2Å</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>, <scene name='pdbligand=MEV:(R)-MEVALONATE'>MEV</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=8tfo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8tfo OCA], [https://pdbe.org/8tfo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8tfo RCSB], [https://www.ebi.ac.uk/pdbsum/8tfo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8tfo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mevalonate kinase is central to the isoprenoid biosynthesis pathway. Here, high-resolution X-ray crystal structures of two mevalonate kinases are presented: a eukaryotic protein from Ramazzottius varieornatus and an archaeal protein from Methanococcoides burtonii. Both enzymes possess the highly conserved motifs of the GHMP enzyme superfamily, with notable differences between the two enzymes in the N-terminal part of the structures. Biochemical characterization of the two enzymes revealed major differences in their sensitivity to geranyl pyrophosphate and farnesyl pyrophosphate, and in their thermal stabilities. This work adds to the understanding of the structural basis of enzyme inhibition and thermostability in mevalonate kinases. | ||
| - | + | Characterization of novel mevalonate kinases from the tardigrade Ramazzottius varieornatus and the psychrophilic archaeon Methanococcoides burtonii.,Esquirol L, Newman J, Nebl T, Scott C, Vickers C, Sainsbury F, Peat TS Acta Crystallogr D Struct Biol. 2024 Mar 1;80(Pt 3):203-215. doi: , 10.1107/S2059798324001360. Epub 2024 Feb 27. PMID:38411551<ref>PMID:38411551</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8tfo" style="background-color:#fffaf0;"></div> |
| - | [[Category: Esquirol | + | == References == |
| - | [[Category: Newman | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Scott | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Ramazzottius varieornatus]] |
| + | [[Category: Esquirol L]] | ||
| + | [[Category: Nebl T]] | ||
| + | [[Category: Newman J]] | ||
| + | [[Category: Peat TS]] | ||
| + | [[Category: Sainsbury F]] | ||
| + | [[Category: Scott C]] | ||
| + | [[Category: Vickers C]] | ||
Current revision
Structure of MKvar
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