2a1r: Difference between revisions

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New page: left|200px<br /> <applet load="2a1r" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a1r, resolution 2.60Å" /> '''Crystal structure o...
 
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[[Image:2a1r.gif|left|200px]]<br />
[[Image:2a1r.gif|left|200px]]<br /><applet load="2a1r" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2a1r" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2a1r, resolution 2.60&Aring;" />
caption="2a1r, resolution 2.60&Aring;" />
'''Crystal structure of PARN nuclease domain'''<br />
'''Crystal structure of PARN nuclease domain'''<br />


==Overview==
==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.
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==
2A1R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=2A1R OCA].  
2A1R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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=2A1R OCA].  


==Reference==
==Reference==
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[[Category: parn]]
[[Category: parn]]


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