2BOV

Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase

「1WCA」から置き換えられました

2BOV の概要

• エントリーDOI: 10.2210/pdb2bov/pdb
• 関連するPDBエントリー: 1G24 1GZE 1GZF 1UAD 1UZI
• 分子名称: RAS-RELATED PROTEIN RAL-A, MONO-ADP-RIBOSYLTRANSFERASE C3, GUANOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: c3bot, exoenzyme, rala, gtpase, adp, ribosylating toxin, gtp-binding, lipoprotein, prenylation, glycosyltransferase, nad, transferase
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cell surface: P11233; Secreted: P15879
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51948.52

構造登録者

Holbourn, K.P.,Sutton, J.M.,Evans, H.R.,Shone, C.C.,Acharya, K.R. (登録日: 2005-04-14, 公開日: 2005-04-15, 最終更新日: 2023-12-13)

主引用文献

Holbourn, K.P.,Sutton, J.M.,Evans, H.R.,Shone, C.C.,Acharya, K.R.
Molecular Recognition of an Adp-Ribosylating Clostridium Botulinum C3 Exoenzyme by Rala Gtpase
Proc.Natl.Acad.Sci.USA, 102:5357-, 2005

PubMed Abstract: C3 exoenzymes (members of the ADP-ribosyltranferase family) are produced by Clostridium botulinum (C3bot1 and -2), Clostridium limosum (C3lim), Bacillus cereus (C3cer), and Staphylococcus aureus (C3stau1-3). These exoenzymes lack a translocation domain but are known to specifically inactivate Rho GTPases in host target cells. Here, we report the crystal structure of C3bot1 in complex with RalA (a GTPase of the Ras subfamily) and GDP at a resolution of 2.66 A. RalA is not ADP-ribosylated by C3 exoenzymes but inhibits ADP-ribosylation of RhoA by C3bot1, C3lim, and C3cer to different extents. The structure provides an insight into the molecular interactions between C3bot1 and RalA involving the catalytic ADP-ribosylating turn-turn (ARTT) loop from C3bot1 and helix alpha4 and strand beta6 (which are not part of the GDP-binding pocket) from RalA. The structure also suggests a molecular explanation for the different levels of C3-exoenzyme inhibition by RalA and why RhoA does not bind C3bot1 in this manner.

PubMed: 15809419
DOI: 10.1073/PNAS.0501525102

実験手法

X-RAY DIFFRACTION (2.66 Å)