Crystal structure of human nicotinamide mononucleotide adenylyltransferase in complex with NMN.

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Werner E,Ziegler M,Lerner F,Schweiger M,Heinemann U

doi

10.1016/s0014-5793(02)02556-5

keywords:

subject

Has Abstract

pub_date

2002-04-10 00:00:00

pages

239-44

issue

1-3

eissn

0014-5793

issn

1873-3468

pii

S0014579302025565

journal_volume

516

pub_type

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