1tp7
From Proteopedia
(New page: 200px<br /><applet load="1tp7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tp7, resolution 2.4Å" /> '''Crystal Structure of ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1tp7.gif|left|200px]]<br /><applet load="1tp7" size=" | + | [[Image:1tp7.gif|left|200px]]<br /><applet load="1tp7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tp7, resolution 2.4Å" /> | caption="1tp7, resolution 2.4Å" /> | ||
'''Crystal Structure of the RNA-dependent RNA Polymerase from Human Rhinovirus 16'''<br /> | '''Crystal Structure of the RNA-dependent RNA Polymerase from Human Rhinovirus 16'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Picornaviruses utilize virally encoded RNA polymerase and a uridylylated | + | Picornaviruses utilize virally encoded RNA polymerase and a uridylylated protein primer to ensure replication of the entire viral genome. The molecular details of this mechanism are not well understood due to the lack of structural information. We report the crystal structure of human rhinovirus 16 3D RNA-dependent RNA polymerase (HRV16 3Dpol) at a 2.4-A resolution, representing the first complete polymerase structure from the Picornaviridae family. HRV16 3Dpol shares the canonical features of other known polymerase structures and contains an N-terminal region that tethers the fingers and thumb subdomains, forming a completely encircled active site cavity which is accessible through a small tunnel on the backside of the molecule. The small thumb subdomain contributes to the formation of a large cleft on the front face of the polymerase which also leads to the active site. The cleft appears large enough to accommodate a template:primer duplex during RNA elongation or a protein primer during the uridylylation stage of replication initiation. Based on the structural features of HRV16 3Dpo1 and the catalytic mechanism known for all polymerases, a front-loading model for uridylylation is proposed. |
==About this Structure== | ==About this Structure== | ||
| - | 1TP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_2 Human rhinovirus 2] with SO4 and DMX as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Full crystallographic information is available from [http:// | + | 1TP7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_rhinovirus_2 Human rhinovirus 2] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=DMX:'>DMX</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/RNA-directed_RNA_polymerase RNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.48 2.7.7.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TP7 OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: RNA-directed RNA polymerase]] | [[Category: RNA-directed RNA polymerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Appleby, T | + | [[Category: Appleby, T C.]] |
| - | [[Category: Cheney, I | + | [[Category: Cheney, I W.]] |
[[Category: Hong, Z.]] | [[Category: Hong, Z.]] | ||
[[Category: Luecke, H.]] | [[Category: Luecke, H.]] | ||
| - | [[Category: Shim, J | + | [[Category: Shim, J H.]] |
[[Category: Vogeley, L.]] | [[Category: Vogeley, L.]] | ||
| - | [[Category: Wu, J | + | [[Category: Wu, J Z.]] |
[[Category: Yao, N.]] | [[Category: Yao, N.]] | ||
[[Category: Zhong, W.]] | [[Category: Zhong, W.]] | ||
| Line 30: | Line 30: | ||
[[Category: rna]] | [[Category: rna]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:53 2008'' |
Revision as of 13:15, 21 February 2008
|
Crystal Structure of the RNA-dependent RNA Polymerase from Human Rhinovirus 16
Overview
Picornaviruses utilize virally encoded RNA polymerase and a uridylylated protein primer to ensure replication of the entire viral genome. The molecular details of this mechanism are not well understood due to the lack of structural information. We report the crystal structure of human rhinovirus 16 3D RNA-dependent RNA polymerase (HRV16 3Dpol) at a 2.4-A resolution, representing the first complete polymerase structure from the Picornaviridae family. HRV16 3Dpol shares the canonical features of other known polymerase structures and contains an N-terminal region that tethers the fingers and thumb subdomains, forming a completely encircled active site cavity which is accessible through a small tunnel on the backside of the molecule. The small thumb subdomain contributes to the formation of a large cleft on the front face of the polymerase which also leads to the active site. The cleft appears large enough to accommodate a template:primer duplex during RNA elongation or a protein primer during the uridylylation stage of replication initiation. Based on the structural features of HRV16 3Dpo1 and the catalytic mechanism known for all polymerases, a front-loading model for uridylylation is proposed.
About this Structure
1TP7 is a Single protein structure of sequence from Human rhinovirus 2 with and as ligands. Active as RNA-directed RNA polymerase, with EC number 2.7.7.48 Full crystallographic information is available from OCA.
Reference
Crystal structure of complete rhinovirus RNA polymerase suggests front loading of protein primer., Appleby TC, Luecke H, Shim JH, Wu JZ, Cheney IW, Zhong W, Vogeley L, Hong Z, Yao N, J Virol. 2005 Jan;79(1):277-88. PMID:15596823
Page seeded by OCA on Thu Feb 21 15:15:53 2008
Categories: Human rhinovirus 2 | RNA-directed RNA polymerase | Single protein | Appleby, T C. | Cheney, I W. | Hong, Z. | Luecke, H. | Shim, J H. | Vogeley, L. | Wu, J Z. | Yao, N. | Zhong, W. | DMX | SO4 | 3d | Polymerase | Rhinovirus | Rna
