High energy exchange: proteins that make or break phosphoramidate bonds

Citation
Vl. Robinson et Am. Stock, High energy exchange: proteins that make or break phosphoramidate bonds, STRUCT F D, 7(3), 1999, pp. R47-R53
Citations number
24
Categorie Soggetti
Biochemistry & Biophysics
Journal title
STRUCTURE WITH FOLDING & DESIGN
ISSN journal
09692126 → ACNP
Volume
7
Issue
3
Year of publication
1999
Pages
R47 - R53
Database
ISI
SICI code
0969-2126(19990315)7:3<R47:HEEPTM>2.0.ZU;2-I
Abstract
Several proteins that catalyze phosphoryl transfer reactions involving phos phohistidine residues have recently been structurally characterized. The ar chitecture of two histidine kinases defines a new protein kinase fold. The diverse folds of several phosphotransfer proteins appear to be designed to foster protein-protein interactions between transfer partners.