5HM2

Crystal structure of the 3C protease from South African Territories type 2 foot-and-mouth disease virus

Summary for 5HM2

• Entry DOI: 10.2210/pdb5hm2/pdb
• Descriptor: 3C proteinase (1 entity in total)
• Functional Keywords: picornavirus, 3c protease, trypsin-like protease, hydrolase
• Biological source: Foot-and-mouth disease virus - type SAT 2
• Total number of polymer chains: 5
• Total formula weight: 112034.55

Authors

Yang, J.,Leen, E.N.,Curry, S. (deposition date: 2016-01-15, release date: 2016-03-02, Last modification date: 2024-01-10)

Primary citation

Yang, J.,Leen, E.N.,Maree, F.F.,Curry, S.
Crystal structure of the 3C protease from Southern African Territories type 2 foot-and-mouth disease virus.
Peerj, 4:e1964-e1964, 2016

PubMed Abstract: The replication of foot-and-mouth disease virus (FMDV) is dependent on the virus-encoded 3C protease (3C(pro)). As in other picornaviruses, 3C(pro) performs most of the proteolytic processing of the polyprotein expressed from the large open reading frame in the RNA genome of the virus. Previous work revealed that the 3C(pro) from serotype A-one of the seven serotypes of FMDV-adopts a trypsin-like fold. On the basis of capsid sequence comparisons the FMDV serotypes are grouped into two phylogenetic clusters, with O, A, C, and Asia 1 in one, and the three Southern African Territories serotypes, (SAT-1, SAT-2 and SAT-3) in another, a grouping pattern that is broadly, but not rigidly, reflected in 3C(pro) amino acid sequences. We report here the cloning, expression and purification of 3C proteases from four SAT serotype viruses (SAT2/GHA/8/91, SAT1/NIG/5/81, SAT1/UGA/1/97, and SAT2/ZIM/7/83) and the crystal structure at 3.2 Å resolution of 3C(pro) from SAT2/GHA/8/91.

PubMed: 27168976
DOI: 10.7717/peerj.1964

Experimental method

X-RAY DIFFRACTION (3.2 Å)