1xup

<table><tr><td colspan='2'>[[1xup]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptococcus_casseliflavus"_vaughan_et_al._1979 "streptococcus casseliflavus" vaughan et al. 1979]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1XUP FirstGlance]. <br>

</td></tr><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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r59|1r59]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glpK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37734 "Streptococcus casseliflavus" Vaughan et al. 1979])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xup FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xup OCA], [http://pdbe.org/1xup PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xup RCSB], [http://www.ebi.ac.uk/pdbsum/1xup PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xup ProSAT]</span></td></tr>

[[http://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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== Publication Abstract from PubMed ==

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.

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:14717590<ref>PMID:14717590</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1xup" style="background-color:#fffaf0;"></div>

[[Category: Streptococcus casseliflavus vaughan et al. 1979]]

[[Category: Glycerol kinase]]

[[Category: Charrier, V]]

[[Category: Darbon, E]]

[[Category: Deutscher, J]]

[[Category: Hol, W G.J]]

[[Category: Hou, L]]

[[Category: Paulo, J]]

[[Category: Yeh, J I]]

[[Category: Transferase]]