2LAF

NMR solution structure of the N-terminal domain of the E. coli lipoprotein BamC

2LAF の概要

• エントリーDOI: 10.2210/pdb2laf/pdb
• 関連するPDBエントリー: 2LAE
• 分子名称: Lipoprotein 34 (1 entity in total)
• 機能のキーワード: beta-barrel assembly machinery, bam, bamc, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane ; Lipid-anchor : P0A903
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26998.98

構造登録者

Pardi, A.,Warner, L. (登録日: 2011-03-11, 公開日: 2011-06-01, 最終更新日: 2024-05-01)

主引用文献

Warner, L.R.,Varga, K.,Lange, O.F.,Baker, S.L.,Baker, D.,Sousa, M.C.,Pardi, A.
Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set.
J.Mol.Biol., 411:83-95, 2011

PubMed Abstract: The CS-RDC-NOE Rosetta program was used to generate the solution structure of a 27-kDa fragment of the Escherichia coli BamC protein from a limited set of NMR data. The BamC protein is a component of the essential five-protein β-barrel assembly machine in E. coli. The first 100 residues in BamC were disordered in solution. The Rosetta calculations showed that BamC₁₀₁₋₃₄₄ forms two well-defined domains connected by an ~18-residue linker, where the relative orientation of the domains was not defined. Both domains adopt a helix-grip fold previously observed in the Bet v 1 superfamily. ¹⁵N relaxation data indicated a high degree of conformational flexibility for the linker connecting the N-terminal domain and the C-terminal domain in BamC. The results here show that CS-RDC-NOE Rosetta is robust and has a high tolerance for misassigned nuclear Overhauser effect restraints, greatly simplifying NMR structure determinations.

PubMed: 21624375
DOI: 10.1016/j.jmb.2011.05.022

実験手法

SOLUTION NMR