1h38: Difference between revisions

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[[Image:1h38.gif|left|200px]]
{{Seed}}
[[Image:1h38.png|left|200px]]


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{{STRUCTURE_1h38|  PDB=1h38  |  SCENE=  }}  
{{STRUCTURE_1h38|  PDB=1h38  |  SCENE=  }}  


'''STRUCTURE OF A T7 RNA POLYMERASE ELONGATION COMPLEX AT 2.9A RESOLUTION'''
===STRUCTURE OF A T7 RNA POLYMERASE ELONGATION COMPLEX AT 2.9A RESOLUTION===




==Overview==
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The single-subunit bacteriophage T7 RNA polymerase carries out the transcription cycle in an identical manner to that of bacterial and eukaryotic multisubunit enzymes. Here we report the crystal structure of a T7 RNA polymerase elongation complex, which shows that incorporation of an 8-base-pair RNA-DNA hybrid into the active site of the enzyme induces a marked rearrangement of the amino-terminal domain. This rearrangement involves alternative folding of about 130 residues and a marked reorientation (about 130 degrees rotation) of a stable core subdomain, resulting in a structure that provides elements required for stable transcription elongation. A wide opening on the enzyme surface that is probably an RNA exit pathway is formed, and the RNA-DNA hybrid is completely buried in a newly formed, deep protein cavity. Binding of 10 base pairs of downstream DNA is stabilized mostly by long-distance electrostatic interactions. The structure implies plausible mechanisms for the various phases of the transcription cycle, and reveals important structural similarities with the multisubunit RNA polymerases.
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==About this Structure==
==About this Structure==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: T7 rna polymerase]]
[[Category: T7 rna polymerase]]
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