2k14

Solution structure of the soluble domain of the NfeD protein YuaF from Bacillus subtilis

spinqualitylabelsall models 2k14 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2k14 is a 1 chain structure with sequence from Bacillus subtilis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NFED2_BACSU Plays a role in assembly of FloT membrane rafts, probably recruited to rafts by FloT. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Solution structure of the soluble domain of the NfeD protein YuaF from Bacillus subtilis.,Walker CA, Hinderhofer M, Witte DJ, Boos W, Moller HM J Biomol NMR. 2008 Aug 12. PMID:18696230 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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