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1oha
From Proteopedia
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Revision as of 13:49, 30 October 2007
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ACETYLGLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH MGADP AND N-ACETYL-L-GLUTAMATE
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
1OHA is a [Single protein] structure of sequence from [Escherichia coli] with ACT, MG, ADP and NLG 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
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Categories: Acetylglutamate kinase | Escherichia coli | Single protein | Fita, I. | Gil-Ortiz, F. | Ramon-Maiques, S. | Rubio, V. | ACT | ADP | MG | NLG | Amino acid kinase | Arginine metabolism | Group transfer | N-acetyl-l-glutamate kinase | Nag kinase | Phosphoryl n-acetyl-l-glutamate 5-phosphotransferase | X-ray diffraction
