2jgv: Difference between revisions
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==STRUCTURE OF | |||
==STRUCTURE OF Staphylococcus aureus D-TAGATOSE-6-PHOSPHATE KINASE in complex with ADP== | |||
<StructureSection load='2jgv' size='340' side='right' caption='[[2jgv]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2jgv' size='340' side='right' caption='[[2jgv]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jg1|2jg1]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jg1|2jg1]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tagatose-6-phosphate_kinase Tagatose-6-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.144 2.7.1.144] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tagatose-6-phosphate_kinase Tagatose-6-phosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.144 2.7.1.144] </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=2jgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jgv OCA], [http://pdbe.org/2jgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jgv RCSB], [http://www.ebi.ac.uk/pdbsum/2jgv PDBsum]</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=2jgv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jgv OCA], [http://pdbe.org/2jgv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jgv RCSB], [http://www.ebi.ac.uk/pdbsum/2jgv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jgv ProSAT]</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/jg/2jgv_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jg/2jgv_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> | ||
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[[Category: Hunter, W N]] | [[Category: Hunter, W N]] | ||
[[Category: Leonard, G A]] | [[Category: Leonard, G A]] | ||
[[Category: | [[Category: McSweeney, S M]] | ||
[[Category: Miallau, L]] | [[Category: Miallau, L]] | ||
[[Category: Conformational change]] | [[Category: Conformational change]] | ||
Revision as of 10:14, 11 July 2018
STRUCTURE OF Staphylococcus aureus D-TAGATOSE-6-PHOSPHATE KINASE in complex with ADPSTRUCTURE OF Staphylococcus aureus D-TAGATOSE-6-PHOSPHATE KINASE in complex with ADP
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 PubMedHigh resolution structures of Staphylococcus aureus d-tagatose-6-phosphate kinase (LacC) in two crystal forms are herein reported. The structures define LacC in apoform, in binary complexes with ADP or the co-factor analogue AMP-PNP, and in a ternary complex with AMP-PNP and D-tagatose-6-phosphate. The tertiary structure of the LacC monomer, which is closely related to other members of the pfkB subfamily of carbohydrate kinases, is composed of a large alpha/beta core domain and a smaller, largely beta "lid." Four extended polypeptide segments connect these two domains. Dimerization of LacC occurs via interactions between lid domains, which come together to form a beta-clasp structure. Residues from both subunits contribute to substrate binding. LacC adopts a closed structure required for phosphoryl transfer only when both substrate and co-factor are bound. A reaction mechanism similar to that used by other phosphoryl transferases is proposed, although unusually, when both substrate and co-factor are bound to the enzyme two Mg(2+) ions are observed in the active site. A new motif of amino acid sequence conservation common to the pfkB subfamily of carbohydrate kinases is identified. Structures of Staphylococcus aureus D-tagatose-6-phosphate kinase implicate domain motions in specificity and mechanism.,Miallau L, Hunter WN, McSweeney SM, Leonard GA J Biol Chem. 2007 Jul 6;282(27):19948-57. Epub 2007 Apr 25. PMID:17459874[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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