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Binding mode of the oxidized α-anomer of NAD+ to RSP, a Rex-family repressor.

Abstract：

:The Rex-family repressors sense redox levels by alternative binding to NADH or NAD(+). RSP is the homologue of Rex in Thermoanaerobacter ethanolicus JW200(T) and regulates ethanol fermentation in this obligate anaerobe. The dimeric repressor binds to DNA by an open conformation. The crystal structure of RSP/α-NAD(+) complex shows a different set of ligand interactions mainly due to the unique configuration of the nicotinamide moiety. The positively charged ring is covered by the Tyr102 side chain and interacts with a sulfate ion adjacent to the N-terminus of helix α8. Consequently, the RSP dimer may be locked in a closed conformation that does not bind to DNA. However, α-NAD(+) does not show a higher affinity to RSP than β-NAD(+). It has to be improved for possible use as an effector in modulating the repressor.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Zheng Y,Ko TP,Yang Y,Shao W,Guo RT

doi

10.1016/j.bbrc.2014.12.049

subject

Has Abstract

pub_date

2015-01-16 00:00:00

pages

733-6

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(14)02215-3

journal_volume

456

pub_type

杂志文章

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