1tp7: Difference between revisions

Line 1:

[[Image:1tp7.gif|left|200px]]<br /><applet load="1tp7" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1tp7.gif|left|200px]]<br /><applet load="1tp7" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1tp7, resolution 2.4Å" />

'''Crystal Structure of the RNA-dependent RNA Polymerase from Human Rhinovirus 16'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1TP7 OCA].

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==

Line 14:

[[Category: RNA-directed RNA polymerase]]

[[Category: Single protein]]

[[Category: Appleby, T.C.]]

[[Category: Appleby, T C.]]

[[Category: Cheney, I.W.]]

[[Category: Cheney, I W.]]

[[Category: Hong, Z.]]

[[Category: Luecke, H.]]

[[Category: Shim, J.H.]]

[[Category: Shim, J H.]]

[[Category: Vogeley, L.]]

[[Category: Wu, J.Z.]]

[[Category: Wu, J Z.]]

[[Category: Yao, N.]]

[[Category: Zhong, W.]]

Line 30:

[[Category: rna]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:53 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1tp7.gif|left|200px]]<br /><applet load="1tp7" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1tp7.gif|left|200px]]<br /><applet load="1tp7" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1tp7, resolution 2.4&Aring;" />
 '''Crystal Structure of the RNA-dependent RNA Polymerase from Human Rhinovirus 16'''<br />
 ==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.
+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==
-TP7 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TP7 OCA].
+TP7 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==
@@ Line 14: / Line 14: @@
 [[Category: RNA-directed RNA polymerase]]
 [[Category: Single protein]]
-[[Category: Appleby, T.C.]]
+[[Category: Appleby, T C.]]
-[[Category: Cheney, I.W.]]
+[[Category: Cheney, I W.]]
 [[Category: Hong, Z.]]
 [[Category: Luecke, H.]]
-[[Category: Shim, J.H.]]
+[[Category: Shim, J H.]]
 [[Category: Vogeley, L.]]
-[[Category: Wu, J.Z.]]
+[[Category: Wu, J Z.]]
 [[Category: Yao, N.]]
 [[Category: Zhong, W.]]
@@ Line 30: / Line 30: @@
 [[Category: rna]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:28:47 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:53 2008''