1gzu: Difference between revisions

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[[Image:1gzu.jpg|left|200px]]
{{Seed}}
[[Image:1gzu.png|left|200px]]


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{{STRUCTURE_1gzu|  PDB=1gzu  |  SCENE=  }}  
{{STRUCTURE_1gzu|  PDB=1gzu  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF HUMAN NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE IN COMPLEX WITH NMN'''
===CRYSTAL STRUCTURE OF HUMAN NICOTINAMIDE MONONUCLEOTIDE ADENYLYLTRANSFERASE IN COMPLEX WITH NMN===




==Overview==
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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.
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{{ABSTRACT_PUBMED_11959140}}


==About this Structure==
==About this Structure==
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[[Category: Adenylyltransferase]]
[[Category: Adenylyltransferase]]
[[Category: Nad biosynthesis]]
[[Category: Nad biosynthesis]]
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