1UZI

C3 EXOENZYME FROM CLOSTRIDIUM BOTULINUM, TETRAGONAL FORM

1UZI の概要

• エントリーDOI: 10.2210/pdb1uzi/pdb
• 関連するPDBエントリー: 1G24 1GZE 1GZF
• 分子名称: MONO-ADP-RIBOSYLTRANSFERASE C3, CYCLO-TETRAMETAVANADATE, VANADATE ION, ... (5 entities in total)
• 機能のキーワード: transferase, c3, adp-ribosyltransferase
• 由来する生物種: CLOSTRIDIUM BOTULINUM
• 細胞内の位置: Secreted: P15879
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48108.70

構造登録者

Evans, H.R.,Holloway, D.E.,Sutton, J.M.,Ayriss, J.,Shone, C.C.,Acharya, K.R. (登録日: 2004-03-12, 公開日: 2004-07-29, 最終更新日: 2023-12-13)

主引用文献

Evans, H.R.,Holloway, D.E.,Sutton, J.M.,Ayriss, J.,Shone, C.C.,Acharya, K.R.
C3 Exoenzyme from Clostridium Botulinum: Structure of a Tetragonal Crystal Form and a Reassessment of Nad-Induced Flexure
Acta Crystallogr.,Sect.D, 60:1502-, 2004

PubMed Abstract: C3 exoenzyme from Clostridium botulinum (C3bot1) ADP-ribosylates and thereby inactivates Rho A, B and C GTPases in mammalian cells. The structure of a tetragonal crystal form has been determined by molecular replacement and refined to 1.89 A resolution. It is very similar to the apo structures determined previously from two different monoclinic crystal forms. An objective reassessment of available apo and nucleotide-bound C3bot1 structures indicates that, contrary to a previous report, the protein possesses a rigid core formed largely of beta-strands and that the general flexure that accompanies NAD binding is concentrated in two peripheral lobes. Tetragonal crystals disintegrate in the presence of NAD, most likely because of disruption of essential crystal contacts.

PubMed: 15272191
DOI: 10.1107/S0907444904011680

実験手法

X-RAY DIFFRACTION (1.89 Å)