 |
InterPro: IPR000577 Carbohydrate kinase, FGGY
Additional Reading
|
|
Feese M, Pettigrew DW, Meadow ND, Roseman S, Remington SJ.
Cation-promoted association of a regulatory and target protein is controlled by protein phosphorylation.
Proc. Natl. Acad. Sci. U.S.A. 91 1994 3544-8
[PubMed: 8170944]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8170944&action=stream&blobtype=pdf
|
|
Yeh JI, Charrier V, Paulo J, Hou L, Darbon E, Claiborne A, Hol WG, Deutscher J.
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.
Biochemistry 43 2004 362-73
[PubMed: 14717590]
http://dx.doi.org/10.1021/bi034258o
|
|
Feese MD, Faber HR, Bystrom CE, Pettigrew DW, Remington SJ.
Glycerol kinase from Escherichia coli and an Ala65-->Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation.
Structure 6 1998 1407-18
[PubMed: 9817843]
http://dx.doi.org/10.1016/S0969-2126(98)00140-3
|
|
Bystrom CE, Pettigrew DW, Branchaud BP, O'Brien P, Remington SJ.
Crystal structures of Escherichia coli glycerol kinase variant S58-->W in complex with nonhydrolyzable ATP analogues reveal a putative active conformation of the enzyme as a result of domain motion.
Biochemistry 38 1999 3508-18
[PubMed: 10090737]
http://dx.doi.org/10.1021/bi982460z
|
|
Ormo M, Bystrom CE, Remington SJ.
Crystal structure of a complex of Escherichia coli glycerol kinase and an allosteric effector fructose 1,6-bisphosphate.
Biochemistry 37 1998 16565-72
[PubMed: 9843423]
http://dx.doi.org/10.1021/bi981616s
|
|
|
InterPro 23.1
|