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| [[Image:1r59.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1r59| PDB=1r59 | SCENE= }} | | {{STRUCTURE_1r59| PDB=1r59 | SCENE= }} |
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| '''Enterococcus casseliflavus glycerol kinase'''
| | ===Enterococcus casseliflavus glycerol kinase=== |
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| ==Overview==
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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. | | The line below this paragraph, {{ABSTRACT_PUBMED_14717590}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14717590 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14717590}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Yeh, J I.]] | | [[Category: Yeh, J I.]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:05:41 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:08:33 2008'' |
