2K3M

Rv1761c

2K3M の概要

• エントリーDOI: 10.2210/pdb2k3m/pdb
• NMR情報: BMRB: 15774
• 分子名称: Rv1761c, S-[(1-oxyl-2,2,5,5-tetramethyl-2,5-dihydro-1H-pyrrol-3-yl)methyl] methanesulfonothioate (2 entities in total)
• 機能のキーワード: protein, integral membrane protein, membrane protein
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17028.65

構造登録者

Page, R.C.,Moore, J.D.,Lee, S.,Opella, S.J.,Cross, T.A. (登録日: 2008-05-14, 公開日: 2009-01-06, 最終更新日: 2024-10-09)

主引用文献

Page, R.C.,Lee, S.,Moore, J.D.,Opella, S.J.,Cross, T.A.
Backbone structure of a small helical integral membrane protein: A unique structural characterization.
Protein Sci., 18:134-146, 2009

PubMed Abstract: The structural characterization of small integral membrane proteins pose a significant challenge for structural biology because of the multitude of molecular interactions between the protein and its heterogeneous environment. Here, the three-dimensional backbone structure of Rv1761c from Mycobacterium tuberculosis has been characterized using solution NMR spectroscopy and dodecylphosphocholine (DPC) micelles as a membrane mimetic environment. This 127 residue single transmembrane helix protein has a significant (10 kDa) C-terminal extramembranous domain. Five hundred and ninety distance, backbone dihedral, and orientational restraints were employed resulting in a 1.16 A rmsd backbone structure with a transmembrane domain defined at 0.40 A. The structure determination approach utilized residual dipolar coupling orientation data from partially aligned samples, long-range paramagnetic relaxation enhancement derived distances, and dihedral restraints from chemical shift indices to determine the global fold. This structural model of Rv1761c displays some influences by the membrane mimetic illustrating that the structure of these membrane proteins is dictated by a combination of the amino acid sequence and the protein's environment. These results demonstrate both the efficacy of the structural approach and the necessity to consider the biophysical properties of membrane mimetics when interpreting structural data of integral membrane proteins and, in particular, small integral membrane proteins.

PubMed: 19177358
DOI: 10.1002/pro.24

実験手法

SOLUTION NMR