C3 exoenzyme from Clostridium botulinum: Structure of a tetragonal crystal form and a reassessment of NAD-induced flexure

Hazel R. Evans, Daniel E. Holloway, J. Mark Sutton, Joanne Ayriss, Clifford C. Shone, K. Ravi Acharya*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)

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 Å 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 β-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.

Original languageEnglish
Pages (from-to)1502-1505
Number of pages4
JournalActa Crystallographica Section D: Biological Crystallography
Volume60
Issue number8
DOIs
Publication statusPublished - Aug 2004

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