This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ohb
From Proteopedia
|
ACETYLGLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ADP AND SULPHATE
Overview
N-Acetyl-L-glutamate kinase (NAGK), the structural paradigm of the enzymes, of the amino acid kinase family, catalyzes the phosphorylation of the, gamma-COO(-) group of N-acetyl-L-glutamate (NAG) by ATP. We determine here, the crystal structures of NAGK complexes with MgADP, NAG and the, transition-state analog AlF(4)(-); with MgADP and NAG; and with ADP and, SO(4)(2-). Comparison of these structures with that of the MgAMPPNP-NAG, complex allows to delineate three successive steps during phosphoryl, transfer: at the beginning, when the attacking and leaving O atoms and the, P atom are imperfectly aligned and the distance between the attacking O, atom and the P atom is 2.8A; midway, at the bipyramidal intermediate, with, nearly perfect alignment and a distance of 2.3A; and, when the ... [(full description)]
About this Structure
1OHB is a [Single protein] structure of sequence from [Escherichia coli] with SO4, ACT and ADP as [ligands]. Active as [Acetylglutamate kinase], with EC number [2.7.2.8]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
The course of phosphorus in the reaction of N-acetyl-L-glutamate kinase, determined from the structures of crystalline complexes, including a complex with an AlF(4)(-) transition state mimic., Gil-Ortiz F, Ramon-Maiques S, Fita I, Rubio V, J Mol Biol. 2003 Aug 1;331(1):231-44. PMID:12875848
Page seeded by OCA on Tue Oct 30 14:08:18 2007
