1gzu
From Proteopedia
CRYSTAL STRUCTURE OF HUMAN NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE IN COMPLEX WITH NMN
Overview
The final step in the biosynthesis of nicotinamide-adenine dinucleotide, a major coenzyme in cellular redox reactions and involved in intracellular signaling, is catalyzed by the enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT). The X-ray structure of human NMNAT in complex with nicotinamide mononucleotide was solved by the single-wavelength anomalous dispersion method at a resolution of 2.9 A. Human NMNAT is a symmetric hexamer whose subunit is formed by a large six-stranded parallel beta-sheet with helices on both sides. Human NMNAT displays a different oligomerization compared to the archaeal enzyme. The protein-nicotinamide mononucleotide interaction pattern provides insight into ligand binding in the human enzyme.
About this Structure
1GZU is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1gry. Full crystallographic information is available from OCA.
Reference
Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN., Werner E, Ziegler M, Lerner F, Schweiger M, Heinemann U, FEBS Lett. 2002 Apr 10;516(1-3):239-44. PMID:11959140 Page seeded by OCA on Fri May 2 18:14:04 2008
