1xup

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[[Image:1xup.jpg|left|200px]]
 
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==ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL==
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The line below this paragraph, containing "STRUCTURE_1xup", creates the "Structure Box" on the page.
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<StructureSection load='1xup' size='340' side='right'caption='[[1xup]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1xup| PDB=1xup | SCENE= }}
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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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'''ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL'''
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==See Also==
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*[[Glycerol kinase|Glycerol kinase]]
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== References ==
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==Overview==
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<references/>
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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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__TOC__
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</StructureSection>
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==About this Structure==
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1XUP is a [[Single protein]] structure of sequence from [http://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].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/14717590 14717590]
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[[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: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:31:58 2008''
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Current revision

ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL

PDB ID 1xup

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