Structure of a NAD kinase from Thermotoga maritima at 2.3 A resolution

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Vaheh OganesyanSung-Hou Kim

Abstract

NAD kinase is the only known enzyme that catalyzes the formation of NADP, a coenzyme involved in most anabolic reactions and in the antioxidant defense system. Despite its importance, very little is known regarding the mechanism of catalysis and only recently have several NAD kinase structures been deposited in the PDB. Here, an independent investigation of the crystal structure of inorganic polyphosphate/ATP-NAD kinase, PPNK_THEMA, a protein from Thermotoga maritima, is reported at a resolution of 2.3 A. The crystal structure was solved using single-wavelength anomalous diffraction (SAD) data collected at the Se absorption-peak wavelength in a state in which no cofactors or substrates were bound. It revealed that the 258-amino-acid protein is folded into two distinct domains, similar to recently reported NAD kinases. The N-terminal alpha/beta-domain spans the first 100 amino acids and the last 30 amino acids of the polypeptide and has several topological matches in the PDB, whereas the other domain, which spans the middle 130 residues, adopts a unique beta-sandwich architecture and only appreciably matches the recently deposited PDB structures of NAD kinases.

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Citations

Jul 7, 2011·The Journal of Biological Chemistry·Takuya AndoKousaku Murata
Jun 27, 2014·PloS One·Wen-Yan LiKun-Ming Chen
Oct 27, 2016·European Journal of Medicinal Chemistry·Julie PaolettiSylvie Pochet
Apr 9, 2008·Bioscience, Biotechnology, and Biochemistry·Shigeyuki Kawai, Kousaku Murata
Feb 14, 2007·The Biochemical Journal·Nadine PollakMathias Ziegler
Oct 12, 2021·Proceedings of the Japan Academy. Series B, Physical and Biological Sciences·Kousaku Murata

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