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 2.75Å" /> '''ENTEROCOCCUS CASSELI...)
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Revision as of 04:14, 21 November 2007
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ENTEROCOCCUS CASSELIFLAVUS GLYCEROL KINASE COMPLEXED WITH GLYCEROL
Overview
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.
About this Structure
1XUP is a Single protein structure of sequence from Enterococcus casseliflavus with GOL as ligand. Active as Glycerol kinase, with EC number 2.7.1.30 Full crystallographic information is available from OCA.
Reference
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
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