1UZI

C3 EXOENZYME FROM CLOSTRIDIUM BOTULINUM, TETRAGONAL FORM

Summary for 1UZI

• Entry DOI: 10.2210/pdb1uzi/pdb
• Related: 1G24 1GZE 1GZF
• Descriptor: MONO-ADP-RIBOSYLTRANSFERASE C3, CYCLO-TETRAMETAVANADATE, VANADATE ION, ... (5 entities in total)
• Functional Keywords: transferase, c3, adp-ribosyltransferase
• Biological source: CLOSTRIDIUM BOTULINUM
• Cellular location: Secreted: P15879
• Total number of polymer chains: 2
• Total formula weight: 48108.70

Authors

Evans, H.R.,Holloway, D.E.,Sutton, J.M.,Ayriss, J.,Shone, C.C.,Acharya, K.R. (deposition date: 2004-03-12, release date: 2004-07-29, Last modification date: 2023-12-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.89 Å)