2YM9

SipD from Salmonella typhimurium

2YM9 の概要

• エントリーDOI: 10.2210/pdb2ym9/pdb
• 関連するPDBエントリー: 2YM0 3ZQB 3ZQE
• 分子名称: CELL INVASION PROTEIN SIPD, SULFATE ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: cell invasion, type 3 secretion, t3ss, needle tip protein, host pathogen interaction, bacterial pathogenesis, tip complex
• 由来する生物種: SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM
• 細胞内の位置: Secreted: Q56026
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 150166.08

構造登録者

Lunelli, M.,Kolbe, M. (登録日: 2011-06-06, 公開日: 2011-08-17, 最終更新日: 2023-12-20)

主引用文献

Lunelli, M.,Hurwitz, R.,Lambers, J.,Kolbe, M.
Crystal Structure of Prgi-Sipd: Insight Into a Secretion Competent State of the Type Three Secretion System Needle Tip and its Interaction with Host Ligands
Plos Pathog., 7:02163-, 2011

PubMed Abstract: Many infectious gram-negative bacteria, including Salmonella typhimurium, require a Type Three Secretion System (T3SS) to translocate virulence factors into host cells. The T3SS consists of a membrane protein complex and an extracellular needle together that form a continuous channel. Regulated secretion of virulence factors requires the presence of SipD at the T3SS needle tip in S. typhimurium. Here we report three-dimensional structures of individual SipD, SipD in fusion with the needle subunit PrgI, and of SipD:PrgI in complex with the bile salt, deoxycholate. Assembly of the complex involves major conformational changes in both SipD and PrgI. This rearrangement is mediated via a π bulge in the central SipD helix and is stabilized by conserved amino acids that may allow for specificity in the assembly and composition of the tip proteins. Five copies each of the needle subunit PrgI and SipD form the T3SS needle tip complex. Using surface plasmon resonance spectroscopy and crystal structure analysis we found that the T3SS needle tip complex binds deoxycholate with micromolar affinity via a cleft formed at the SipD:PrgI interface. In the structure-based three-dimensional model of the T3SS needle tip, the bound deoxycholate faces the host membrane. Recently, binding of SipD with bile salts present in the gut was shown to impede bacterial infection. Binding of bile salts to the SipD:PrgI interface in this particular arrangement may thus inhibit the T3SS function. The structures presented in this study provide insight into the open state of the T3SS needle tip. Our findings present the atomic details of the T3SS arrangement occurring at the pathogen-host interface.

PubMed: 21829362
DOI: 10.1371/JOURNAL.PPAT.1002163

実験手法

X-RAY DIFFRACTION (3 Å)