PDBsum entry 2k14

Unknown function

PDB id: 2k14

Contents

Protein chain

84 a.a. *

* Residue conservation analysis

PDB id:

2k14

Name:

Unknown function

Title:

Solution structure of the soluble domain of the nfed protein yuaf from bacillus subtilis

Structure:

Yuaf protein. Chain: a. Fragment: c-terminal domain (unp residues 97-174). Engineered: yes

Source:

Bacillus subtilis. Strain: marburg 168. Gene: yuaf. Expressed in: escherichia coli. Other_details: the plasmid phiho1421 was constructed by fusing the coding sequence of residues 97-174 of yuaf to the 3'-end of the male gene containing an additional thrombin cleavage site. The solublE C- terminal domain of yuaf was generated by cleaving off the male part by digestion with thrombin.

NMR struc:

20 models

Authors:

C.A.Walker,M.Hinderhofer,D.J.Witte,W.Boos,H.M.Moller

Key ref:

C.A.Walker et al. (2008). Solution structure of the soluble domain of the NfeD protein YuaF from Bacillus subtilis. J Biomol Nmr, 42, 69-76. PubMed id: 18696230

Date:

20-Feb-08 Release date: 26-Aug-08

Protein chain

O32077  (NFED2_BACSU) -  Membrane protein NfeD2 from Bacillus subtilis (strain 168)

Seq: 174 a.a.

Struc: 84 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.?

J Biomol Nmr 42:69-76 (2008)

PubMed id: 18696230

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

C.A.Walker, M.Hinderhofer, D.J.Witte, W.Boos, H.M.Möller.

ABSTRACT

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.