Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis.

Abstract:

:As a member of the dynamin superfamily human guanylate-binding protein 1 (hGBP1) binds and hydrolyses GTP thereby undergoing structural changes which lead to self-assembly of the protein. Here, we employ the reactivity of hGBP1 with a cysteine reactive compound in order to monitor structural changes imposed by GTP binding and hydrolysis. Positions of cysteine residues buried between the C-terminal domain of hGBP1 and the rest of the protein are identified which report a large change of accessibility by the compound after addition of GTP. Our results indicate that nucleotide hydrolysis induces a domain movement in hGBP1, which we suggest enables further assembly of the protein.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Vöpel T,Kunzelmann S,Herrmann C

doi

10.1016/j.febslet.2009.05.027

subject

Has Abstract

pub_date

2009-06-18 00:00:00

pages

1923-7

issue

12

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(09)00399-8

journal_volume

583

pub_type

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