2qcy: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= rep ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 SARS coronavirus]) | |GENE= rep ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 SARS coronavirus]) | ||
|DOMAIN= | |DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam05409 Peptidase_C30]</span> | ||
|RELATEDENTRY=[[2qc2|2QC2]] | |RELATEDENTRY=[[2qc2|2QC2]] | ||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qcy OCA], [http://www.ebi.ac.uk/pdbsum/2qcy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qcy RCSB]</span> | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qcy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qcy OCA], [http://www.ebi.ac.uk/pdbsum/2qcy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2qcy RCSB]</span> | ||
| Line 14: | Line 14: | ||
'''Crystal Structure of a monomeric form of Severe Acute Respiratory Syndrome (SARS) 3C-like protease mutant''' | '''Crystal Structure of a monomeric form of Severe Acute Respiratory Syndrome (SARS) 3C-like protease mutant''' | ||
==Overview== | |||
Unlike 3C protease, the SARS-CoV 3C-like protease (3CLpro) is only enzymatically active as a homodimer and its catalysis is under extensive regulation by the unique extra domain. Despite intense studies, two puzzles still remain: 1) how dimer-monomer switch is controlled; and 2) why dimerization is absolutely required for catalysis. Here we report the monomeric crystal structure of the SARS-CoV 3CLpro mutant R298A at a resolution of 1.75 A. Detailed analysis reveals that Arg298 serves as a key component for maintaining dimerization and consequently its mutation will trigger a cooperative switch from dimer to monomer. The monomeric enzyme is irreversibly inactivated because its catalytic machinery is frozen in the collapsed state, characteristic of the formation of a short 310-helix from an active-site loop. Remarkably, dimerization appears to be coupled to catalysis in 3CLpro through use of overlapped residues for two networks, one for dimerization and another for the catalysis. | |||
==About this Structure== | ==About this Structure== | ||
2QCY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QCY OCA]. | 2QCY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QCY OCA]. | ||
==Reference== | |||
Mechanism for Controlling Dimer-monomer Switch and Coupling Dimerization to Catalysis of the SARS-CoV 3C-Like Protease., Shi J, Sivaraman J, Song J, J Virol. 2008 Feb 27;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18305031 18305031] | |||
[[Category: Sars coronavirus]] | [[Category: Sars coronavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 30: | Line 36: | ||
[[Category: n-finger]] | [[Category: n-finger]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 2 11:31:56 2008'' | ||
