Abstract:
: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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Yeh JI,Charrier V,Paulo J,Hou L,Darbon E,Claiborne A,Hol WG,Deutscher Jdoi
10.1021/bi034258osubject
Has Abstractpub_date
2004-01-20 00:00:00pages
362-73issue
2eissn
0006-2960issn
1520-4995journal_volume
43pub_type
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