3W5J

Crystal structure of GDP-bound NfeoB from Gallionella capsiferriformans

Summary for 3W5J

• Entry DOI: 10.2210/pdb3w5j/pdb
• Related: 3W5I
• Descriptor: Ferrous iron transport protein B, GUANOSINE-5'-DIPHOSPHATE, GLYCEROL, ... (5 entities in total)
• Functional Keywords: g protein, iron transport, gtpase, transmembrane, gdp, metal transport
• Biological source: Gallionella capsiferriformans
• Total number of polymer chains: 2
• Total formula weight: 46095.95

Authors

Deshpande, C.N.,McGrath, A.P.,Jormakka, M. (deposition date: 2013-01-30, release date: 2013-04-24, Last modification date: 2023-11-08)

Primary citation

Deshpande, C.N.,McGrath, A.P.,Font, J.,Guilfoyle, A.P.,Maher, M.J.,Jormakka, M.
Structure of an atypical FeoB G-domain reveals a putative domain-swapped dimer.
Acta Crystallogr.,Sect.F, 69:399-404, 2013

PubMed 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 Fe(2+) 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.

PubMed: 23545645
DOI: 10.1107/S1744309113005939

Experimental method

X-RAY DIFFRACTION (1.932 Å)