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

Evans HR, Holloway DE, Sutton JM, Ayriss J, Shone CC, Acharya KR
Acta Crystallogr D Biol Crystallogr 60 1502-5 (2004)
Cited: 12 times
EuropePMC logo PMID: 15272191

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.

Reviews - 1uzi mentioned but not cited (2)

  1. The use of polyoxometalates in protein crystallography - An attempt to widen a well-known bottleneck. Bijelic A, Rompel A. Coord Chem Rev 299 22-38 (2015)
  2. Interaction of Vanadium Complexes with Proteins: Revisiting the Reported Structures in the Protein Data Bank (PDB) since 2015. Santos MFA, Pessoa JC. Molecules 28 6538 (2023)

Articles - 1uzi mentioned but not cited (2)

  1. Polyoxometalates: more than a phasing tool in protein crystallography. Bijelic A, Rompel A. ChemTexts 4 10 (2018)
  2. The complexity of protein interactions unravelled from structural disorder. Seoane B, Carbone A. PLoS Comput Biol 17 e1008546 (2021)


Reviews citing this publication (3)

  1. Clostridial toxins. Popoff MR, Bouvet P. Future Microbiol 4 1021-1064 (2009)
  2. Bacterial factors exploit eukaryotic Rho GTPase signaling cascades to promote invasion and proliferation within their host. Popoff MR. Small GTPases 5 e28209 (2014)
  3. Variations in the Botulinum Neurotoxin Binding Domain and the Potential for Novel Therapeutics. Davies JR, Liu SM, Acharya KR. Toxins (Basel) 10 E421 (2018)

Articles citing this publication (5)

  1. Molecular recognition of an ADP-ribosylating Clostridium botulinum C3 exoenzyme by RalA GTPase. Holbourn KP, Sutton JM, Evans HR, Shone CC, Acharya KR. Proc Natl Acad Sci U S A 102 5357-5362 (2005)
  2. Confirmation of botulism in birds and cattle by the mouse bioassay and Endopep-MS. Hedeland M, Moura H, Båverud V, Woolfitt AR, Bondesson U, Barr JR. J Med Microbiol 60 1299-1305 (2011)
  3. Structure-function discrepancy in Clostridium botulinum C3 toxin for its rational prioritization as a subunit vaccine. Prathiviraj R, Prisilla A, Chellapandi P. J Biomol Struct Dyn 34 1317-1329 (2016)
  4. Equine grass sickness, but not botulism, causes autonomic and enteric neurodegeneration and increases soluble N-ethylmaleimide-sensitive factor attachment receptor protein expression within neuronal perikarya. McGorum BC, Scholes S, Milne EM, Eaton SL, Wishart TM, Poxton IR, Moss S, Wernery U, Davey T, Harris JB, Pirie RS. Equine Vet J 48 786-791 (2016)
  5. Editorial Equine grass sickness: Benefits of a multifaceted research approach. Pirie RS, McGorum BC. Equine Vet J 48 770-772 (2016)


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