2BW2

BofC from Bacillus subtilis

2BW2 の概要

• エントリーDOI: 10.2210/pdb2bw2/pdb
• NMR情報: BMRB: 6731
• 分子名称: BYPASS OF FORESPORE C (1 entity in total)
• 機能のキーワード: sporulation, signaling protein, bofc, sigmak checkpoint
• 由来する生物種: BACILLUS SUBTILIS
• 細胞内の位置: Forespore intermembrane space: O05391
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16195.25

構造登録者

Patterson, H.M.,Brannigan, J.A.,Cutting, S.M.,Wilson, K.S.,Wilkinson, A.J.,Ab, E.,Diercks, T.,Folkers, G.E.,de Jong, R.N.,Truffault, V.,Kaptein, R. (登録日: 2005-07-08, 公開日: 2005-09-15, 最終更新日: 2024-05-15)

主引用文献

Patterson, H.M.,Brannigan, J.A.,Cutting, S.M.,Wilson, K.S.,Wilkinson, A.J.,Ab, E.,Diercks, T.,de Jong, R.N.,Truffault, V.,Folkers, G.E.,Kaptein, R.
The structure of bypass of forespore C, an intercompartmental signaling factor during sporulation in Bacillus.
J. Biol. Chem., 280:36214-36220, 2005

PubMed Abstract: Sporulation in Bacillus subtilis begins with an asymmetric cell division giving rise to smaller forespore and larger mother cell compartments. Different programs of gene expression are subsequently directed by compartment-specific RNA polymerase sigma-factors. In the final stages, spore coat proteins are synthesized in the mother cell under the control of RNA polymerase containing sigma(K), (Esigma(K)). sigma(K) is synthesized as an inactive zymogen, pro-sigma(K), which is activated by proteolytic cleavage. Processing of pro-sigma(K) is performed by SpoIVFB, a metalloprotease that resides in a complex with SpoIVFA and bypass of forespore (Bof)A in the outer forespore membrane. Ensuring coordination of events taking place in the two compartments, pro-sigma(K) processing in the mother cell is delayed until appropriate signals are received from the forespore. Cell-cell signaling is mediated by SpoIVB and BofC, which are expressed in the forespore and secreted to the intercompartmental space where they regulate pro-sigma(K) processing by mechanisms that are not yet fully understood. Here we present the three-dimensional structure of BofC determined by solution state NMR. BofC is a monomer made up of two domains. The N-terminal domain, containing a four-stranded beta-sheet onto one face of which an alpha-helix is packed, closely resembles the third immunoglobulin-binding domain of protein G from Streptococcus. The C-terminal domain contains a three-stranded beta-sheet and three alpha-helices in a novel domain topology. The sequence connecting the domains contains a conserved DISP motif to which mutations that affect BofC activity map. Possible roles for BofC in the sigma(K) checkpoint are discussed in the light of sequence and structure comparisons.

PubMed: 16049010
DOI: 10.1074/jbc.M506910200

実験手法

SOLUTION NMR