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(New page: 200px<br /><applet load="2fav" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fav, resolution 1.800Å" /> '''Crystal structure o...) |
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'''Crystal structure of SARS macro domain in complex with ADP-ribose at 1.8 A resolution'''<br /> | '''Crystal structure of SARS macro domain in complex with ADP-ribose at 1.8 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Macro domains constitute a protein module family found associated with | + | 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== | ==About this Structure== | ||
| - | 2FAV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus] with APR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2FAV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_sars_coronavirus Human sars coronavirus] with <scene name='pdbligand=APR:'>APR</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FAV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human sars coronavirus]] | [[Category: Human sars coronavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Egloff, M | + | [[Category: Egloff, M P.]] |
| - | [[Category: MSGP, Marseilles | + | [[Category: MSGP, Marseilles Structural Genomics Program.@.AFMB.]] |
[[Category: Malet, H.]] | [[Category: Malet, H.]] | ||
[[Category: APR]] | [[Category: APR]] | ||
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[[Category: structural proteomics in europe]] | [[Category: structural proteomics in europe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:19:28 2008'' |
Revision as of 15:19, 21 February 2008
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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 with as ligand. 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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