2a1r
From Proteopedia
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[[Image:2a1r.gif|left|200px]] | [[Image:2a1r.gif|left|200px]] | ||
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'''Crystal structure of PARN nuclease domain''' | '''Crystal structure of PARN nuclease domain''' | ||
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Structural insight into poly(A) binding and catalytic mechanism of human PARN., Wu M, Reuter M, Lilie H, Liu Y, Wahle E, Song H, EMBO J. 2005 Dec 7;24(23):4082-93. Epub 2005 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16281054 16281054] | Structural insight into poly(A) binding and catalytic mechanism of human PARN., Wu M, Reuter M, Lilie H, Liu Y, Wahle E, Song H, EMBO J. 2005 Dec 7;24(23):4082-93. Epub 2005 Nov 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16281054 16281054] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Poly(A)-specific ribonuclease]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Song, H.]] | [[Category: Song, H.]] | ||
[[Category: Wu, M.]] | [[Category: Wu, M.]] | ||
| - | [[Category: | + | [[Category: Dedd]] |
| - | [[Category: | + | [[Category: Nuclease domain]] |
| - | [[Category: | + | [[Category: Parn]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:29:41 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:29, 3 May 2008
Crystal structure of PARN nuclease domain
Overview
Poly(A)-specific ribonuclease (PARN) is a processive, poly(A)-specific 3' exoribonuclease. The crystal structure of C-terminal truncated human PARN determined in two states (free and RNA-bound forms) reveals that PARNn is folded into two domains, an R3H domain and a nuclease domain similar to those of Pop2p and epsilon186. The high similarity of the active site structures of PARNn and epsilon186 suggests that they may have a similar catalytic mechanism. PARNn forms a tight homodimer, with the R3H domain of one subunit partially enclosing the active site of the other subunit and poly(A) bound in a deep cavity of its nuclease domain in a sequence-nonspecific manner. The R3H domain and, possibly, the cap-binding domain are involved in poly(A) binding but these domains alone do not appear to contribute to poly(A) specificity. Mutations disrupting dimerization abolish both the enzymatic and RNA-binding activities, suggesting that the PARN dimer is a structural and functional unit. The cap-binding domain may act in concert with the R3H domain to amplify the processivity of PARN.
About this Structure
2A1R is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural insight into poly(A) binding and catalytic mechanism of human PARN., Wu M, Reuter M, Lilie H, Liu Y, Wahle E, Song H, EMBO J. 2005 Dec 7;24(23):4082-93. Epub 2005 Nov 10. PMID:16281054 Page seeded by OCA on Sat May 3 18:29:41 2008
Categories: Homo sapiens | Single protein | Song, H. | Wu, M. | Dedd | Nuclease domain | Parn
