2fav
From Proteopedia
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|PDB= 2fav |SIZE=350|CAPTION= <scene name='initialview01'>2fav</scene>, resolution 1.800Å | |PDB= 2fav |SIZE=350|CAPTION= <scene name='initialview01'>2fav</scene>, resolution 1.800Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene> | + | |LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= NSP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Human SARS coronavirus]) | |GENE= NSP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Human SARS coronavirus]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fav OCA], [http://www.ebi.ac.uk/pdbsum/2fav PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fav RCSB]</span> | ||
}} | }} | ||
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[[Category: MSGP, Marseilles Structural Genomics Program.@.AFMB.]] | [[Category: MSGP, Marseilles Structural Genomics Program.@.AFMB.]] | ||
[[Category: Malet, H.]] | [[Category: Malet, H.]] | ||
- | [[Category: APR]] | ||
[[Category: marseilles structural genomics program @ afmb]] | [[Category: marseilles structural genomics program @ afmb]] | ||
[[Category: msgp]] | [[Category: msgp]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:00:12 2008'' |
Revision as of 00:00, 31 March 2008
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, resolution 1.800Å | |||||||
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Ligands: | , | ||||||
Gene: | NSP3 (Human SARS coronavirus) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of SARS macro domain in complex with ADP-ribose at 1.8 A resolution
Overview
Macro domains constitute a protein module family found associated with specific histones and proteins involved in chromatin metabolism. In addition, a small number of animal RNA viruses, such as corona- and toroviruses, alphaviruses, and hepatitis E virus, encode macro domains for which, however, structural and functional information is extremely limited. Here, we characterized the macro domains from hepatitis E virus, Semliki Forest virus, and severe acute respiratory syndrome coronavirus (SARS-CoV). The crystal structure of the SARS-CoV macro domain was determined at 1.8-Angstroms resolution in complex with ADP-ribose. Information derived from structural, mutational, and sequence analyses suggests a close phylogenetic and, most probably, functional relationship between viral and cellular macro domain homologs. The data revealed that viral macro domains have relatively poor ADP-ribose 1"-phosphohydrolase activities (which were previously proposed to be their biologically relevant function) but bind efficiently free and poly(ADP-ribose) polymerase 1-bound poly(ADP-ribose) in vitro. Collectively, these results suggest to further evaluate the role of viral macro domains in host response to viral infection.
About this Structure
2FAV is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.
Reference
Structural and functional basis for ADP-ribose and poly(ADP-ribose) binding by viral macro domains., Egloff MP, Malet H, Putics A, Heinonen M, Dutartre H, Frangeul A, Gruez A, Campanacci V, Cambillau C, Ziebuhr J, Ahola T, Canard B, J Virol. 2006 Sep;80(17):8493-502. PMID:16912299
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