4LSO

Crystal structure of the soluble domain of a Type IV secretion system protein VirB8 from Bartonella quintana Toulouse

4LSO の概要

• エントリーDOI: 10.2210/pdb4lso/pdb
• 関連するPDBエントリー: 4jf8 4kz1
• 分子名称: Type IV secretion system protein virB8 (2 entities in total)
• 機能のキーワード: structural genomics, niaid, national institute of allergy and infectious diseases, seattle structural genomics center for infectious disease, ssgcid, dimer-monomer analysis, type iv secretion system, innate response, human pathogen, host specific protein, cell adhesion, protein transport
• 由来する生物種: Bartonella quintana
• 細胞内の位置: Cell inner membrane ; Single- pass membrane protein : Q6FYW3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 20890.49

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2013-07-22, 公開日: 2014-03-05, 最終更新日: 2023-09-20)

主引用文献

Gillespie, J.J.,Phan, I.Q.,Scheib, H.,Subramanian, S.,Edwards, T.E.,Lehman, S.S.,Piitulainen, H.,Rahman, M.S.,Rennoll-Bankert, K.E.,Staker, B.L.,Taira, S.,Stacy, R.,Myler, P.J.,Azad, A.F.,Pulliainen, A.T.
Structural Insight into How Bacteria Prevent Interference between Multiple Divergent Type IV Secretion Systems.
MBio, 6:e01867-e01815, 2015

PubMed Abstract: Prokaryotes use type IV secretion systems (T4SSs) to translocate substrates (e.g., nucleoprotein, DNA, and protein) and/or elaborate surface structures (i.e., pili or adhesins). Bacterial genomes may encode multiple T4SSs, e.g., there are three functionally divergent T4SSs in some Bartonella species (vir, vbh, and trw). In a unique case, most rickettsial species encode a T4SS (rvh) enriched with gene duplication. Within single genomes, the evolutionary and functional implications of cross-system interchangeability of analogous T4SS protein components remains poorly understood. To lend insight into cross-system interchangeability, we analyzed the VirB8 family of T4SS channel proteins. Crystal structures of three VirB8 and two TrwG Bartonella proteins revealed highly conserved C-terminal periplasmic domain folds and dimerization interfaces, despite tremendous sequence divergence. This implies remarkable structural constraints for VirB8 components in the assembly of a functional T4SS. VirB8/TrwG heterodimers, determined via bacterial two-hybrid assays and molecular modeling, indicate that differential expression of trw and vir systems is the likely barrier to VirB8-TrwG interchangeability. We also determined the crystal structure of Rickettsia typhi RvhB8-II and modeled its coexpressed divergent paralog RvhB8-I. Remarkably, while RvhB8-I dimerizes and is structurally similar to other VirB8 proteins, the RvhB8-II dimer interface deviates substantially from other VirB8 structures, potentially preventing RvhB8-I/RvhB8-II heterodimerization. For the rvh T4SS, the evolution of divergent VirB8 paralogs implies a functional diversification that is unknown in other T4SSs. Collectively, our data identify two different constraints (spatiotemporal for Bartonella trw and vir T4SSs and structural for rvh T4SSs) that mediate the functionality of multiple divergent T4SSs within a single bacterium.

PubMed: 26646013
DOI: 10.1128/mBio.01867-15

実験手法

X-RAY DIFFRACTION (1.7 Å)