1s0v
From Proteopedia
(New page: 200px<br /><applet load="1s0v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s0v, resolution 3.2Å" /> '''Structural basis for ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1s0v.gif|left|200px]]<br /><applet load="1s0v" size=" | + | [[Image:1s0v.gif|left|200px]]<br /><applet load="1s0v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1s0v, resolution 3.2Å" /> | caption="1s0v, resolution 3.2Å" /> | ||
'''Structural basis for substrate selection by T7 RNA polymerase'''<br /> | '''Structural basis for substrate selection by T7 RNA polymerase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The mechanism by which nucleotide polymerases select the correct substrate | + | The mechanism by which nucleotide polymerases select the correct substrate is of fundamental importance to the fidelity of DNA replication and transcription. During the nucleotide addition cycle, pol I DNA polymerases undergo the transition from a catalytically inactive "open" to an active "closed" conformation. All known determinants of substrate selection are associated with the "closed" state. To elucidate if this mechanism is conserved in homologous single subunit RNA polymerases (RNAPs), we have determined the structure of T7 RNAP elongation complex with the incoming substrate analog. Surprisingly, the substrate specifically binds to RNAP in the "open" conformation, where it is base paired with the acceptor template base, while Tyr639 provides discrimination of ribose versus deoxyribose substrates. The structure therefore suggests a novel mechanism, in which the substrate selection occurs prior to the isomerization to the catalytically active conformation. Modeling of multisubunit RNAPs suggests that this mechanism might be universal for all RNAPs. |
==About this Structure== | ==About this Structure== | ||
| - | 1S0V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7] with MG and APC as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http:// | + | 1S0V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=APC:'>APC</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/DNA-directed_RNA_polymerase DNA-directed RNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.6 2.7.7.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S0V OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Anikin, M.]] | [[Category: Anikin, M.]] | ||
| - | [[Category: McAllister, W | + | [[Category: McAllister, W T.]] |
[[Category: Patlan, V.]] | [[Category: Patlan, V.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Temiakov, D.]] | [[Category: Temiakov, D.]] | ||
| - | [[Category: Vassylyev, D | + | [[Category: Vassylyev, D G.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: APC]] | [[Category: APC]] | ||
| Line 30: | Line 30: | ||
[[Category: t7 rna polymerase]] | [[Category: t7 rna polymerase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:41 2008'' |
Revision as of 12:56, 21 February 2008
|
Structural basis for substrate selection by T7 RNA polymerase
Overview
The mechanism by which nucleotide polymerases select the correct substrate is of fundamental importance to the fidelity of DNA replication and transcription. During the nucleotide addition cycle, pol I DNA polymerases undergo the transition from a catalytically inactive "open" to an active "closed" conformation. All known determinants of substrate selection are associated with the "closed" state. To elucidate if this mechanism is conserved in homologous single subunit RNA polymerases (RNAPs), we have determined the structure of T7 RNAP elongation complex with the incoming substrate analog. Surprisingly, the substrate specifically binds to RNAP in the "open" conformation, where it is base paired with the acceptor template base, while Tyr639 provides discrimination of ribose versus deoxyribose substrates. The structure therefore suggests a novel mechanism, in which the substrate selection occurs prior to the isomerization to the catalytically active conformation. Modeling of multisubunit RNAPs suggests that this mechanism might be universal for all RNAPs.
About this Structure
1S0V is a Single protein structure of sequence from Bacteriophage t7 with and as ligands. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.
Reference
Structural basis for substrate selection by t7 RNA polymerase., Temiakov D, Patlan V, Anikin M, McAllister WT, Yokoyama S, Vassylyev DG, Cell. 2004 Feb 6;116(3):381-91. PMID:15016373
Page seeded by OCA on Thu Feb 21 14:56:41 2008
Categories: Bacteriophage t7 | DNA-directed RNA polymerase | Single protein | Anikin, M. | McAllister, W T. | Patlan, V. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Temiakov, D. | Vassylyev, D G. | Yokoyama, S. | APC | MG | Dna | Riken structural genomics/proteomics initiative | Rna | Rsgi | Structural genomics | T7 rna polymerase
