1xup

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(New page: 200px<br /><applet load="1xup" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xup, resolution 2.75&Aring;" /> '''ENTEROCOCCUS CASSELI...)
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[[Image:1xup.jpg|left|200px]]<br /><applet load="1xup" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1xup, resolution 2.75&Aring;" />
 
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'''ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL'''<br />
 
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==Overview==
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==ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL==
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The first structure of a glycerol kinase from a Gram-positive organism, Enterococcus casseliflavus, has been determined to 2.8 A resolution in the, presence of glycerol and to 2.5 A resolution in the absence of substrate., The substrate-induced closure of 7 degrees is significantly smaller than, that reported for hexokinase, a model for substrate-mediated domain, closure that has been proposed for glycerol kinase. Despite the 78% level, of sequence identity and conformational similarity in the catalytic cleft, regions of the En. casseliflavus and Escherichia coli glycerol kinases, remarkable structural differences have now been identified. These, differences correlate well with their divergent regulatory schemes of, activation by phosphorylation in En. casseliflavus and allosteric, inhibition in E. coli. On the basis of our structural results, we propose, a mechanism by which the phosphorylation of a histidyl residue located 25, A from the active site results in a 10-15-fold increase in the activity of, the enterococcal glycerol kinase.
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<StructureSection load='1xup' size='340' side='right'caption='[[1xup]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1xup]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_casseliflavus Enterococcus casseliflavus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XUP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XUP FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xup OCA], [https://pdbe.org/1xup PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xup RCSB], [https://www.ebi.ac.uk/pdbsum/1xup PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xup ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLPK_ENTCA GLPK_ENTCA] Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.<ref>PMID:9162046</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xu/1xup_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1xup ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1XUP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_casseliflavus Enterococcus casseliflavus] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glycerol_kinase Glycerol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.30 2.7.1.30] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XUP OCA].
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*[[Glycerol kinase|Glycerol kinase]]
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== References ==
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==Reference==
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<references/>
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Structures of enterococcal glycerol kinase in the absence and presence of glycerol: correlation of conformation to substrate binding and a mechanism of activation by phosphorylation., Yeh JI, Charrier V, Paulo J, Hou L, Darbon E, Claiborne A, Hol WG, Deutscher J, Biochemistry. 2004 Jan 20;43(2):362-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14717590 14717590]
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__TOC__
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</StructureSection>
[[Category: Enterococcus casseliflavus]]
[[Category: Enterococcus casseliflavus]]
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[[Category: Glycerol kinase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Charrier V]]
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[[Category: Charrier, V.]]
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[[Category: Darbon E]]
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[[Category: Darbon, E.]]
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[[Category: Deutscher J]]
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[[Category: Deutscher, J.]]
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[[Category: Hol WGJ]]
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[[Category: Hol, W.G.J.]]
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[[Category: Hou L]]
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[[Category: Hou, L.]]
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[[Category: Paulo J]]
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[[Category: Paulo, J.]]
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[[Category: Yeh JI]]
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[[Category: Yeh, J.I.]]
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[[Category: GOL]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:21:34 2007''
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ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL

PDB ID 1xup

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