2JOW

Differences in the electrostatic surfaces of the type III secretion needle proteins

2JOW の概要

• エントリーDOI: 10.2210/pdb2jow/pdb
• NMR情報: BMRB: 15206
• 分子名称: Protein prgI (1 entity in total)
• 機能のキーワード: needle protein, transport protein
• 由来する生物種: Salmonella typhimurium
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9276.26

構造登録者

Wang, Y.,Ouellette, A.N.,Egan, C.W.,De Guzman, R.N. (登録日: 2007-04-06, 公開日: 2007-07-24, 最終更新日: 2024-05-08)

主引用文献

Wang, Y.,Ouellette, A.N.,Egan, C.W.,Rathinavelan, T.,Im, W.,De Guzman, R.N.
Differences in the Electrostatic Surfaces of the Type III Secretion Needle Proteins PrgI, BsaL, and MxiH
J.Mol.Biol., 371:1304-1314, 2007

PubMed Abstract: Gram-negative bacteria use a needle-like protein assembly, the type III secretion apparatus, to inject virulence factors into target cells to initiate human disease. The needle is formed by the polymerization of approximately 120 copies of a small acidic protein that is conserved among diverse pathogens. We previously reported the structure of the BsaL needle monomer from Burkholderia pseudomallei by nuclear magnetic resonance (NMR) spectroscopy and others have determined the crystal structure of the Shigella flexneri MxiH needle. Here, we report the NMR structure of the PrgI needle protein of Salmonella typhimurium, a human pathogen associated with food poisoning. PrgI, BsaL, and MxiH form similar two helix bundles, however, the electrostatic surfaces of PrgI differ radically from those of BsaL or MxiH. In BsaL and MxiH, a large negative area is on a face formed by the helix alpha1-alpha2 interface. In PrgI, the major negatively charged surface is not on the "face" but instead is on the "side" of the two-helix bundle, and only residues from helix alpha1 contribute to this negative region. Despite being highly acidic proteins, these molecules contain large basic regions, suggesting that electrostatic contacts are important in needle assembly. Our results also suggest that needle-packing interactions may be different among these bacteria and provide the structural basis for why PrgI and MxiH, despite 63% sequence identity, are not interchangeable in S. typhimurium and S. flexneri.

PubMed: 17617421
DOI: 10.1016/j.jmb.2007.06.034

実験手法

SOLUTION NMR