Member database | Pfam |
Pfam type | domain |
Short name | PMT_C3 |
Clan | Peptidase_CA |
Author | Lazaro Pinto Beatriz;0000-0001-6837-2941 Chuguransky S;0000-0002-0520-0736 Bateman A;0000-0002-6982-4660 |
Sequence Ontology | 0000417 |
Description
Pasteurella multocida toxin (PMT) inhibits osteoblastic differentiation in mammals and birds. Its N-terminal region binds to target cells, while its C-terminal region, with a Trojan horse-like shape, carries the intracellularly active moiety. The latter consists of three distinct domains: C1 (Pfam:PF11647), C2 and C3. This entry represents the C-terminal catalytic domain C3, which has a Cys-His-Asp triad known to perform acyl-hydrolysis such as peptidase activity or an acyl-transfer reaction. This domain adopts a typical alpha-beta protein fold with seven beta-strands and eight helices. It is organised into two subdomains that form the the biologically active cleft space
[2, 1].
References
1.The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling. Biancucci M, Minasov G, Banerjee A, Herrera A, Woida PJ, Kieffer MB, Bindu L, Abreu-Blanco M, Anderson WF, Gaponenko V, Stephen AG, Holderfield M, Satchell KJF. Sci Signal 11, (2018). PMID: 30279169
2.Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin. Kitadokoro K, Kamitani S, Miyazawa M, Hanajima-Ozawa M, Fukui A, Miyake M, Horiguchi Y. Proc. Natl. Acad. Sci. U.S.A. 104, 5139-44, (2007). View articlePMID: 17360394