2ga9
From Proteopedia
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|PDB= 2ga9 |SIZE=350|CAPTION= <scene name='initialview01'>2ga9</scene>, resolution 2.300Å | |PDB= 2ga9 |SIZE=350|CAPTION= <scene name='initialview01'>2ga9</scene>, resolution 2.300Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SAP:ADENOSINE-5'-DIPHOSPHATE+MONOTHIOPHOSPHATE'>SAP</scene> |
- | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ga9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ga9 OCA], [http://www.ebi.ac.uk/pdbsum/2ga9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ga9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Moure, C M.]] | [[Category: Moure, C M.]] | ||
[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
- | [[Category: CA]] | ||
- | [[Category: SAP]] | ||
[[Category: heterodimer]] | [[Category: heterodimer]] | ||
[[Category: nucleotidyltransferase]] | [[Category: nucleotidyltransferase]] | ||
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[[Category: processivity]] | [[Category: processivity]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:13:56 2008'' |
Revision as of 00:13, 31 March 2008
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, resolution 2.300Å | |||||||
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Ligands: | , | ||||||
Activity: | mRNA (nucleoside-2'-O-)-methyltransferase, with EC number 2.1.1.57 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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