5WTB

Complex Structure of Staphylococcus aureus SdrE with human complement factor H

5WTB の概要

• エントリーDOI: 10.2210/pdb5wtb/pdb
• 関連するPDBエントリー: 5WTA
• 分子名称: Serine-aspartate repeat-containing protein E, Peptide from Complement factor H (2 entities in total)
• 機能のキーワード: staphylococcus aureus, sdr family, complement factor h, complement evasion, cell adhesion
• 由来する生物種: Staphylococcus aureus (strain Mu50 / ATCC 700699); 詳細
• 細胞内の位置: Secreted, cell wall ; Peptidoglycan-anchor : Q932F7; Secreted: P08603
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 160823.95

構造登録者

Wu, M.,Zhang, Y.,Hang, T.,Wang, C.,Yang, Y.,Zang, J.,Zhang, M.,Zhang, X. (登録日: 2016-12-10, 公開日: 2017-07-19, 最終更新日: 2023-11-08)

主引用文献

Zhang, Y.,Wu, M.,Hang, T.,Wang, C.,Yang, Y.,Pan, W.,Zang, J.,Zhang, M.,Zhang, X.
Staphylococcus aureus SdrE captures complement factor H's C-terminus via a novel 'close, dock, lock and latch' mechanism for complement evasion
Biochem. J., 474:1619-1631, 2017

PubMed Abstract: Complement factor H (CFH) is a soluble complement regulatory protein essential for the down-regulation of the alternative pathway on interaction with specific markers on the host cell surface. It recognizes the complement component 3b (C3b) and 3d (C3d) fragments in addition to self cell markers (i.e. glycosaminoglycans, sialic acid) to distinguish host cells that deserve protection from pathogens that should be eliminated. The surface protein serine-aspartate repeat protein E (SdrE) was previously reported to bind human CFH as an immune-evasion tactic. However, the molecular mechanism underlying SdrE-CFH-mediated immune evasion remains unknown. In the present study, we identified a novel region at CFH's C-terminus (CFH), which binds SdrE N2 and N3 domains (SdrE) with high affinity, and determined the crystal structures of apo-SdrE and the SdrE-CFH complex. Comparison of the structure of the CFH-SdrE complex with other CFH structures reveals that CFH's C-terminal tail flips from the main body to insert into the ligand-binding groove of SdrE. In addition, SdrE adopts a 'close' state in the absence of CFH, which undergoes a large conformational change on CFH binding, suggesting a novel 'close, dock, lock and latch' (CDLL) mechanism for SdrE to recognize its ligand. Our findings imply that SdrE functions as a 'clamp' to capture CFH's C-terminal tail via a unique CDLL mechanism and sequesters CFH on the surface of for complement evasion.

PubMed: 28258151
DOI: 10.1042/BCJ20170085

実験手法

X-RAY DIFFRACTION (3.3 Å)