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An unusual conformation of NAD+ bound to sorbitol dehydrogenase? A time-dependent transferred nuclear Overhauser effect study.

Abstract：

:The conformation of NAD+ in the sheep liver sorbitol dehydrogenase-NAD+ binary complex has been investigated using time-dependent proton-proton transferred nuclear Overhauser enhancement measurements to determine interproton distance ratios and distances between bound NAD+ protons. The conformation about both the adenosine and nicotinamide riboside glycosidic bonds is anti, the conformations of the adenosine and nicotinamide ribose rings are C3'-endo and C1'-exo, respectively, and the conformations about the adenosine and nicotinamide riboside C4'-C5' bonds are g+ and t, respectively, similar to those found in complexes of NAD+ with other A type dehydrogenases. In addition, however, the distance data are indicative of an unusual overall conformation of NAD+ in the sorbitol dehydrogenase-NAD+ binary complex, with the planes of the nicotinamide and adenine rings separated by 6 to 8 A and at approximately 120 degrees to each other. This overall conformation differs from the concensus extended conformation found in the NAD+-dehydrogenase complexes crystallized to date, where the planes of the nicotinamide and adenine rings are 12 to 14 A apart and nearly perpendicular to each other.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Gronenborn AM,Clore GM,Jeffery J

doi

10.1016/s0022-2836(84)80023-6

subject

Has Abstract

pub_date

1984-02-05 00:00:00

pages

559-72

issue

4

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(84)80023-6

journal_volume

172

pub_type

杂志文章

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