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PDBsum entry 2k14
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Unknown function
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PDB id
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2k14
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References listed in PDB file
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Key reference
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Title
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Solution structure of the soluble domain of the nfed protein yuaf from bacillus subtilis.
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Authors
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C.A.Walker,
M.Hinderhofer,
D.J.Witte,
W.Boos,
H.M.Möller.
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Ref.
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J Biomol Nmr, 2008,
42,
69-76.
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PubMed id
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Abstract
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The transmembrane protein YuaF from B. subtilis is a member of the NfeD-like
clan with a potential role in maintaining membrane integrity during conditions
of cellular stress. nfeD-genes are primarily found in highly conserved operon
structures together with the gene of another membrane protein belonging to the
SPFH superfamily, in this case YuaG. This strongly suggests a functional if not
physical interaction between YuaF and YuaG. Secondary structure predictions of
NfeD proteins that accompany SPFH proteins all indicate a high content of
beta-sheets in the C-terminal domains indicating a conserved core structure
despite very low homology at the level of primary structure. Here we report the
high-resolution solution structure of YuaF's soluble C-terminal domain derived
from NMR data (sYuaF, residues 97-174 of full-length YuaF). Full backbone and
side chain assignments of sYuaF were obtained from triple-resonance spectra. The
structure was determined from distance restraints derived from 3D NOESY spectra
collected at 600 MHz and 800 MHz, together with phi, psi, and chi(1) torsion
angle restraints based on the analysis of (1)H(N), (15)N, (1)H(alpha),
(13)C(alpha), (13)CO, and (13)C(beta) chemical shifts, and HNHA, HNHB and
HACAHB-COSY spectra. Structures were calculated using CYANA 2.0 and refined in
AMBER 8. sYuaF is composed of an extended N-terminal alpha-helix and a
beta-barrel formed by five beta-strands. This beta-sheet core structure is well
known from the diverse class of OB-fold proteins and can also be found in the
distantly related NfeD protein Ph0471 from the archaeon P. horikoshii. Despite
significant differences of their amino acid sequences the structural homology of
these proteins suggests a conserved function of SPFH-associated NfeD proteins.
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