The NMR structure of the domain II of a chloroplastic NifU-like protein OsNifU1A.

Abstract:

:NifU-like proteins are a highly conserved protein that serves as the scaffold for assembly of Fe-S clusters. Chloroplastic NifU-like proteins have tandem NifU like domains, named domain I and domain II. Although the amino acid sequences of these domains are very similar to each other, the predicted functional region for the Fe-S cluster assembly, the CXXC motif, exists only in domain I. The structure of the domain II of chloroplastic NifU-like protein OsNifU1A has an alpha-beta sandwich structure containing two alpha helices located on one side of the beta-sheet. The electrostatic surface potential of OsNifU1A domain II is predominantly positively charged. Chloroplastic NifU-like proteins are targeted to ferredoxin for transferring the Fe-S cluster. The ferredoxin presents an overall negatively charged surface, which may evoke an electrostatic association with OsNifU1A domain II.

journal_name

J Biomol NMR

authors

Kumeta H,Ogura K,Asayama M,Katoh S,Katoh E,Teshima K,Inagaki F

doi

10.1007/s10858-007-9155-9

subject

Has Abstract

pub_date

2007-06-01 00:00:00

pages

161-4

issue

2

eissn

0925-2738

issn

1573-5001

journal_volume

38

pub_type

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