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1r59

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[[Image:1r59.jpg|left|200px]]<br /><applet load="1r59" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1r59, resolution 2.5&Aring;" />
 
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'''Enterococcus casseliflavus glycerol kinase'''<br />
 
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==Overview==
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==Enterococcus casseliflavus glycerol kinase==
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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='1r59' size='340' side='right'caption='[[1r59]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1r59]] 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=1R59 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R59 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]] 2.5&#8491;</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=1r59 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r59 OCA], [https://pdbe.org/1r59 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r59 RCSB], [https://www.ebi.ac.uk/pdbsum/1r59 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r59 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/r5/1r59_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=1r59 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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1R59 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterococcus_casseliflavus Enterococcus casseliflavus]. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1R59 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: Claiborne A]]
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[[Category: Claiborne, A.]]
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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 WG]]
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[[Category: Hol, W G.]]
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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 Thu Feb 21 14:47:11 2008''
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Current revision

Enterococcus casseliflavus glycerol kinase

PDB ID 1r59

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