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Structure of an atypical FeoB G‐domain reveals a putative domain‐swapped dimer

Structure of an atypical FeoB G‐domain reveals a putative domain‐swapped dimer FeoB is a transmembrane protein involved in ferrous iron uptake in prokaryotic organisms. FeoB comprises a cytoplasmic soluble domain termed NFeoB and a C‐terminal polytopic transmembrane domain. Recent structures of NFeoB have revealed two structural subdomains: a canonical GTPase domain and a five‐helix helical domain. The GTPase domain hydrolyses GTP to GDP through a well characterized mechanism, a process which is required for Fe2+ transport. In contrast, the precise role of the helical domain has not yet been fully determined. Here, the structure of the cytoplasmic domain of FeoB from Gallionella capsiferriformans is reported. Unlike recent structures of NFeoB, the G. capsiferriformans NFeoB structure is highly unusual in that it does not contain a helical domain. The crystal structures of both apo and GDP‐bound protein forms a domain‐swapped dimer. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

Structure of an atypical FeoB G‐domain reveals a putative domain‐swapped dimer

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References (32)

Publisher
Wiley
Copyright
International Union of Crystallography, 2013
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309113005939
pmid
23545645
Publisher site
See Article on Publisher Site

Abstract

FeoB is a transmembrane protein involved in ferrous iron uptake in prokaryotic organisms. FeoB comprises a cytoplasmic soluble domain termed NFeoB and a C‐terminal polytopic transmembrane domain. Recent structures of NFeoB have revealed two structural subdomains: a canonical GTPase domain and a five‐helix helical domain. The GTPase domain hydrolyses GTP to GDP through a well characterized mechanism, a process which is required for Fe2+ transport. In contrast, the precise role of the helical domain has not yet been fully determined. Here, the structure of the cytoplasmic domain of FeoB from Gallionella capsiferriformans is reported. Unlike recent structures of NFeoB, the G. capsiferriformans NFeoB structure is highly unusual in that it does not contain a helical domain. The crystal structures of both apo and GDP‐bound protein forms a domain‐swapped dimer.

Journal

Acta Crystallographica Section FWiley

Published: Apr 1, 2013

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