View source for 3pct


==Structure of the class C acid phosphatase from Pasteurella multocida==
<StructureSection load='3pct' size='340' side='right'caption='[[3pct]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3pct]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pasteurella_multocida Pasteurella multocida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PCT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PCT FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pct OCA], [https://pdbe.org/3pct PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pct RCSB], [https://www.ebi.ac.uk/pdbsum/3pct PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pct ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B9VWB2_PASMD B9VWB2_PASMD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pasteurella multocida is a pathogen of veterinary and medical importance. Here, we report the 1.85A 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.

Crystal structure and immunogenicity of the class C acid phosphatase from Pasteurella multocida.,Singh H, Malinski TJ, Reilly TJ, Henzl MT, Tanner JJ Arch Biochem Biophys. 2011 Mar 1. PMID:21371420<ref>PMID:21371420</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3pct" style="background-color:#fffaf0;"></div>

==See Also==
*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pasteurella multocida]]
[[Category: Malinski TJ]]
[[Category: Reilly TJ]]
[[Category: Singh H]]
[[Category: Tanner JJ]]