2VDW

Guanosine N7 methyl-transferase sub-complex (D1-D12) of the vaccinia virus mRNA capping enzyme

Summary for 2VDW

• Entry DOI: 10.2210/pdb2vdw/pdb
• Descriptor: VACCINIA VIRUS CAPPING ENZYME D1 SUBUNIT, MRNA-CAPPING ENZYME SMALL SUBUNIT, SULFATE ION, ... (4 entities in total)
• Functional Keywords: nucleotidyltransferase, s-adenosyl-l-methionine, rna metabolism, mrna processing, methyltransferase, poxvirus, hydrolase, transferase, mrna capping, s-adenosyl homocysteine, d1-d12 heterodimer, methyl-transferase, mrna capping enzyme, multifunctional enzyme
• Biological source: VACCINIA VIRUS; More
• Total number of polymer chains: 8
• Total formula weight: 275223.16

Authors

De la Pena, M.,Kyrieleis, O.J.P.,Cusack, S. (deposition date: 2007-10-12, release date: 2008-05-13, Last modification date: 2024-05-08)

Primary citation

De La Pena, M.,Kyrieleis, O.J.P.,Cusack, S.
Structural Insights Into the Mechanism and Evolution of the Vaccinia Virus Mrna CAP N7 Methyl- Transferase.
Embo J., 26:4913-, 2007

PubMed Abstract: The vaccinia virus mRNA capping enzyme is a multifunctional heterodimeric protein associated with the viral polymerase that both catalyses the three steps of mRNA capping and regulates gene transcription. The structure of a subcomplex comprising the C-terminal N7-methyl-transferase (MT) domain of the large D1 subunit, the stimulatory D12 subunit and bound S-adenosyl-homocysteine (AdoHcy) has been determined at 2.7 A resolution and reveals several novel features of the poxvirus capping enzyme. The structure shows for the first time the critical role played by the proteolytically sensitive N-terminus of the MT domain in binding the methyl donor and in catalysis. In addition, the poxvirus enzyme has a completely unique mode of binding of the adenosine moiety of AdoHcy, a feature that could be exploited for design of specific anti-poxviral compounds. The structure of the poxvirus-specific D12 subunit suggests that it was originally an RNA cap 2'O-MT that has evolved to a catalytically inactive form that has been retained for D1 stabilisation and MT activity enhancement through an allosteric mechanism.

PubMed: 17989694
DOI: 10.1038/SJ.EMBOJ.7601912

Experimental method

X-RAY DIFFRACTION (2.7 Å)