1v19: Difference between revisions
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==2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS== | ==2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS== | ||
<StructureSection load='1v19' size='340' side='right' caption='[[1v19]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='1v19' size='340' side='right' caption='[[1v19]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v1a|1v1a]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1v1a|1v1a]]</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=1v19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v19 OCA], [http://pdbe.org/1v19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v19 RCSB], [http://www.ebi.ac.uk/pdbsum/1v19 PDBsum], [http://www.topsan.org/Proteins/RSGI/1v19 TOPSAN]</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=1v19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v19 OCA], [http://pdbe.org/1v19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1v19 RCSB], [http://www.ebi.ac.uk/pdbsum/1v19 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1v19 ProSAT], [http://www.topsan.org/Proteins/RSGI/1v19 TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/1v19_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/1v19_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 10:32, 28 March 2018
2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS2-KETO-3-DEOXYGLUCONATE KINASE FROM THERMUS THERMOPHILUS
Structural highlights
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 PubMed2-Keto-3-deoxygluconate kinase (KDGK) catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to 2-keto-3-deoxy-6-phosphogluconate (KDGP). The genome sequence of Thermus thermophilus HB8 contains an open reading frame that has a 30% identity to Escherichia coli KDGK. The KDGK activity of T.thermophilus protein (TtKDGK) has been confirmed, and its crystal structure has been determined by the molecular replacement method and refined with two crystal forms to 2.3 angstroms and 3.2 angstroms, respectively. The enzyme is a hexamer organized as a trimer of dimers. Each subunit is composed of two domains, a larger alpha/beta domain and a smaller beta-sheet domain, similar to that of ribokinase and adenosine kinase, members of the PfkB family of carbohydrate kinases. Furthermore, the TtKDGK structure with its KDG and ATP analogue was determined and refined at 2.1 angstroms. The bound KDG was observed predominantly as an open chain structure. The positioning of ligands and the conservation of important catalytic residues suggest that the reaction mechanism is likely to be similar to that of other members of the PfkB family, including ribokinase. In particular, the Asp251 is postulated to have a role in transferring the gamma-phosphate of ATP to the 5'-hydroxyl group of KDG. Structure of Thermus thermophilus 2-Keto-3-deoxygluconate kinase: evidence for recognition of an open chain substrate.,Ohshima N, Inagaki E, Yasuike K, Takio K, Tahirov TH J Mol Biol. 2004 Jul 9;340(3):477-89. PMID:15210349[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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