1r59
From Proteopedia
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| - | [[Image:1r59.jpg|left|200px]] | + | [[Image:1r59.jpg|left|200px]] |
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| - | '''Enterococcus casseliflavus glycerol kinase''' | + | {{Structure |
| + | |PDB= 1r59 |SIZE=350|CAPTION= <scene name='initialview01'>1r59</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= GLPK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37734 Enterococcus casseliflavus]) | ||
| + | }} | ||
| + | |||
| + | '''Enterococcus casseliflavus glycerol kinase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1R59 is a [ | + | 1R59 is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/14717590 14717590] |
[[Category: Enterococcus casseliflavus]] | [[Category: Enterococcus casseliflavus]] | ||
[[Category: Glycerol kinase]] | [[Category: Glycerol kinase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:47:04 2008'' |
Revision as of 11:47, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Gene: | GLPK (Enterococcus casseliflavus) | ||||||
| Activity: | Glycerol kinase, with EC number 2.7.1.30 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Enterococcus casseliflavus glycerol kinase
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
1R59 is a Single protein structure of sequence from Enterococcus casseliflavus. 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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