Abstract:
:Pasteurella multocida is a pathogen of veterinary and medical importance. Here, we report the 1.85Å resolution crystal structure of the class C acid phosphatase from this organism (denoted rPmCCAP). The structure shows that rPmCCAP exhibits the same haloacid dehalogenase fold and dimeric assembly as the class C enzyme from Haemophilus influenzae. Formation of the dimer in solution is demonstrated using analytical ultracentrifugation. The active site is devoid of a magnesium ion due to the presence of citrate in the crystallization buffer. Absence of the metal ion minimally perturbs the active site structure, which suggests that the main role of the ion is to balance the negative charge of the substrate rather than stabilize the active site structure. The crystal lattice displays unusual crystal packing involving the C-terminal polyhistidine tag mimicking the substrate. Steady-state kinetic constants are determined for the substrates NMN, 5'-AMP, 3'-AMP, 2'-AMP, and p-nitrophenyl phosphate. The highest catalytic efficiency is observed with NMN. The production of polyclonal anti-rPmCCAP antibodies is demonstrated, and these antibodies are shown to cross-react with the H. influenzae class C phosphatase. The antibodies are used to detect PmCCAP in clinical P. multocida and Mannheimia haemolytica strains cultured from infected animals.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Singh H,Malinski TJ,Reilly TJ,Henzl MT,Tanner JJdoi
10.1016/j.abb.2011.02.021subject
Has Abstractpub_date
2011-05-01 00:00:00pages
76-81issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(11)00085-3journal_volume
509pub_type
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