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PDBsum entry 3a1v
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Transport protein
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PDB id
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3a1v
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Contents |
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* Residue conservation analysis
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Structure
17:1345-1355
(2009)
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PubMed id:
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Structural basis of novel interactions between the small-GTPase and GDI-like domains in prokaryotic FeoB iron transporter.
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M.Hattori,
Y.Jin,
H.Nishimasu,
Y.Tanaka,
M.Mochizuki,
T.Uchiumi,
R.Ishitani,
K.Ito,
O.Nureki.
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ABSTRACT
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The FeoB family proteins are widely distributed prokaryotic membrane proteins
involved in Fe(2+) uptake. FeoB consists of N-terminal cytosolic and C-terminal
transmembrane domains. The N-terminal region of the cytosolic domain is
homologous to small GTPase (G) proteins and is considered to regulate Fe(2+)
uptake. The spacer region connecting the G and TM domains reportedly functions
as a GDP dissociation inhibitor (GDI)-like domain that stabilizes the
GDP-binding state. However, the function of the G and GDI-like domains in iron
uptake remains unclear. Here, we report the structural and functional analyses
of the FeoB cytosolic domain from Thermotoga maritima. The structure-based
mutational analysis indicated that the interaction between the G and GDI-like
domains is important for both the GDI and Fe(2+) uptake activities. On the basis
of these results, we propose a regulatory mechanism of Fe(2+) uptake.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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K.W.Hung,
Y.W.Chang,
E.T.Eng,
J.H.Chen,
Y.C.Chen,
Y.J.Sun,
C.D.Hsiao,
G.Dong,
K.A.Spasov,
V.M.Unger,
and
T.H.Huang
(2010).
Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB.
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J Struct Biol,
170,
501-512.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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