2fav: Difference between revisions
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[[Image:2fav.gif|left|200px]] | [[Image:2fav.gif|left|200px]] | ||
'''Crystal structure of SARS macro domain in complex with ADP-ribose at 1.8 A resolution''' | {{Structure | ||
|PDB= 2fav |SIZE=350|CAPTION= <scene name='initialview01'>2fav</scene>, resolution 1.800Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene> | |||
|ACTIVITY= | |||
|GENE= NSP3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Human SARS coronavirus]) | |||
}} | |||
'''Crystal structure of SARS macro domain in complex with ADP-ribose at 1.8 A resolution''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2FAV is a [ | 2FAV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FAV OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16912299 16912299] | ||
[[Category: Human sars coronavirus]] | [[Category: Human sars coronavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: msgp]] | [[Category: msgp]] | ||
[[Category: protein-adp-ribose complex]] | [[Category: protein-adp-ribose complex]] | ||
[[Category: structural | [[Category: structural genomic]] | ||
[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:50:11 2008'' | ||
Revision as of 17:50, 20 March 2008
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| , resolution 1.800Å | |||||||
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| Ligands: | |||||||
| Gene: | NSP3 (Human SARS coronavirus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of SARS macro domain in complex with ADP-ribose at 1.8 A resolution
OverviewOverview
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 StructureAbout this Structure
2FAV is a Single protein structure of sequence from Human sars coronavirus. Full crystallographic information is available from OCA.
ReferenceReference
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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