2ga9

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(New page: 200px<br /><applet load="2ga9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ga9, resolution 2.300&Aring;" /> '''Crystal Structure o...)
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[[Image:2ga9.gif|left|200px]]<br /><applet load="2ga9" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ga9.gif|left|200px]]<br /><applet load="2ga9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ga9, resolution 2.300&Aring;" />
caption="2ga9, resolution 2.300&Aring;" />
'''Crystal Structure of the Heterodimeric Vaccinia Virus Polyadenylate Polymerase with Bound ATP-gamma-S'''<br />
'''Crystal Structure of the Heterodimeric Vaccinia Virus Polyadenylate Polymerase with Bound ATP-gamma-S'''<br />
==Overview==
==Overview==
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Polyadenylation of mRNAs in poxviruses, crucial for virion maturation, is, carried out by a poly(A) polymerase heterodimer composed of a catalytic, component, VP55, and a processivity factor, VP39. The ATP-gamma-S bound, and unbound crystal structures of the vaccinia polymerase reveal an, unusual architecture for VP55 that comprises of N-terminal, central or, catalytic, and C-terminal domains with different topologies and that, differs from many polymerases, including the eukaryotic poly(A), polymerases. Residues in the active site of VP55, located between the, catalytic and C-terminal domains, make specific interactions with the, adenine of the ATP analog, establishing the molecular basis of ATP, recognition. VP55's concave surface docks the globular VP39. A model for, RNA primer binding that involves all three VP55 domains and VP39 is, proposed. The model supports biochemical evidence that VP39 functions as a, processivity factor by partially enclosing the RNA primer at the, heterodimer interface.
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Polyadenylation of mRNAs in poxviruses, crucial for virion maturation, is carried out by a poly(A) polymerase heterodimer composed of a catalytic component, VP55, and a processivity factor, VP39. The ATP-gamma-S bound and unbound crystal structures of the vaccinia polymerase reveal an unusual architecture for VP55 that comprises of N-terminal, central or catalytic, and C-terminal domains with different topologies and that differs from many polymerases, including the eukaryotic poly(A) polymerases. Residues in the active site of VP55, located between the catalytic and C-terminal domains, make specific interactions with the adenine of the ATP analog, establishing the molecular basis of ATP recognition. VP55's concave surface docks the globular VP39. A model for RNA primer binding that involves all three VP55 domains and VP39 is proposed. The model supports biochemical evidence that VP39 functions as a processivity factor by partially enclosing the RNA primer at the heterodimer interface.
==About this Structure==
==About this Structure==
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2GA9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus] with CA and SAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/mRNA_(nucleoside-2'-O-)-methyltransferase mRNA (nucleoside-2'-O-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.57 2.1.1.57] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GA9 OCA].
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2GA9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Vaccinia_virus Vaccinia virus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SAP:'>SAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/mRNA_(nucleoside-2'-O-)-methyltransferase mRNA (nucleoside-2'-O-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.57 2.1.1.57] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GA9 OCA].
==Reference==
==Reference==
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[[Category: Vaccinia virus]]
[[Category: Vaccinia virus]]
[[Category: mRNA (nucleoside-2'-O-)-methyltransferase]]
[[Category: mRNA (nucleoside-2'-O-)-methyltransferase]]
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[[Category: Bowman, B.R.]]
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[[Category: Bowman, B R.]]
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[[Category: Gershon, P.D.]]
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[[Category: Gershon, P D.]]
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[[Category: Moure, C.M.]]
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[[Category: Moure, C M.]]
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[[Category: Quiocho, F.A.]]
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[[Category: Quiocho, F A.]]
[[Category: CA]]
[[Category: CA]]
[[Category: SAP]]
[[Category: SAP]]
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[[Category: processivity]]
[[Category: processivity]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:04:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:29:45 2008''

Revision as of 15:29, 21 February 2008


2ga9, resolution 2.300Å

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Crystal Structure of the Heterodimeric Vaccinia Virus Polyadenylate Polymerase with Bound ATP-gamma-S

Overview

Polyadenylation of mRNAs in poxviruses, crucial for virion maturation, is carried out by a poly(A) polymerase heterodimer composed of a catalytic component, VP55, and a processivity factor, VP39. The ATP-gamma-S bound and unbound crystal structures of the vaccinia polymerase reveal an unusual architecture for VP55 that comprises of N-terminal, central or catalytic, and C-terminal domains with different topologies and that differs from many polymerases, including the eukaryotic poly(A) polymerases. Residues in the active site of VP55, located between the catalytic and C-terminal domains, make specific interactions with the adenine of the ATP analog, establishing the molecular basis of ATP recognition. VP55's concave surface docks the globular VP39. A model for RNA primer binding that involves all three VP55 domains and VP39 is proposed. The model supports biochemical evidence that VP39 functions as a processivity factor by partially enclosing the RNA primer at the heterodimer interface.

About this Structure

2GA9 is a Protein complex structure of sequences from Vaccinia virus with and as ligands. Active as mRNA (nucleoside-2'-O-)-methyltransferase, with EC number 2.1.1.57 Full crystallographic information is available from OCA.

Reference

Crystal structures of the vaccinia virus polyadenylate polymerase heterodimer: insights into ATP selectivity and processivity., Moure CM, Bowman BR, Gershon PD, Quiocho FA, Mol Cell. 2006 May 5;22(3):339-49. PMID:16678106

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