2a1s

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(New page: 200px<br /> <applet load="2a1s" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a1s, resolution 2.60&Aring;" /> '''Crystal structure o...)
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'''Crystal structure of native PARN nuclease domain'''<br />
'''Crystal structure of native PARN nuclease domain'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2A1S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 2A1S with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb86_1.html Exosomes]]. Active as [http://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease Poly(A)-specific ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.13.4 3.1.13.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A1S OCA].
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2A1S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 2A1S with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb86_1.html Exosomes]]. Active as [http://en.wikipedia.org/wiki/Poly(A)-specific_ribonuclease Poly(A)-specific ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.13.4 3.1.13.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A1S OCA].
==Reference==
==Reference==
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[[Category: r3h]]
[[Category: r3h]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:44:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:22:46 2008''

Revision as of 14:22, 21 February 2008


2a1s, resolution 2.60Å

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Crystal structure of native 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

2A1S is a Single protein structure of sequence from Homo sapiens. The following page contains interesting information on the relation of 2A1S with [Exosomes]. Active as Poly(A)-specific ribonuclease, with EC number 3.1.13.4 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

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