RESEARCH ARTICLE


Histidine Residues at the Active Site of the Pasteurella multocida Toxin



Gillian D Pullinger#, Alistair J Lax*
King’s College London, Dental Institute, Department of Microbiology, London SE1 9RT, UK
# Present address: Institute for Animal Health, Compton, Newbury, Berkshire, RG20 7NN, UK


Article Metrics

CrossRef Citations:
7
Total Statistics:

Full-Text HTML Views: 895
Abstract HTML Views: 545
PDF Downloads: 220
Total Views/Downloads: 1660
Unique Statistics:

Full-Text HTML Views: 510
Abstract HTML Views: 381
PDF Downloads: 159
Total Views/Downloads: 1050



Creative Commons License
2007 Bentham Science Publishers Ltd

* Address correspondence to this author at the King’s College London Dental Institute, Department of Microbiology, London SE1 9RT, UK; E-mail: alistair.lax@kcl.ac.uk


Abstract

We have investigated histidine residues near the active site of the mitogenic Pasteurella multocida toxin. Mutation of H1202 or H1228 had little effect, while the effect of mutation on H1223 depended on the amino acid substituted. Mutation of H1205 caused complete loss of activity, indicating its importance in PMT activity.

Keywords: Pasteurella multocida, toxin, PMT, domain structure, histidine residues, G-proteins.