User:Ankit Vahia/sandbox1
From Proteopedia
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<applet load='3E2E' size='[450,338]' frame='true' align='right' | <applet load='3E2E' size='[450,338]' frame='true' align='right' | ||
caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Ankit_Vahia/sandbox1/T7-7mer_rna_scene_2/2'>TextToBeDisplayed</scene> | caption='Aspartate receptor ligand binding domain (1wat)' scene='User:Ankit_Vahia/sandbox1/T7-7mer_rna_scene_2/2'>TextToBeDisplayed</scene> | ||
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| - | === Ligand-binding domain === | ||
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| - | The spinning protein (<scene name='User:Lynmarie_K_Thompson/Sandbox_1/Loadedfrompdb/4'>Initial view</scene>) ) is the ligand binding domain of the aspartate receptor with the aspartate ligand bound (LKT). | ||
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| - | Molecular Playground banner: A receptor protein used by bacteria to "smell" their environment. | ||
Revision as of 16:02, 29 April 2010
[Image:intactModelLargeText.jpg|frame|T7 RNA Polymerase in the Late Initiation Phase]
A CBI Molecule being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
T7 RNA polymerase is a a single sub-unit DNA dependent RNA polymerase from the T7 RNA bacteriophage. Like most RNA polymerase T7 RNA polymerase transcribes DNA through three phases -Initiation -Elongation -Termination
The initiation phase continues until the enzyme synthesizes ~8 base RNA after which it loses promoter contacts and transitions into the stable elongation phase. The initiation phase in T7 RNA polymerase like all other single and multi subunit RNA polymerases is characterized by inherent instability leading to the release of small RNA (3-8 bases long). In addition to the crystal structure of the enzyme with a 3 base DNA-RNA hybrid (PDB ID:1QLN) this 7 base intermediate structure provides an insight into the structural changes within the enzyme has it synthesizes RNA during initiation and provides an insight into the mechanism that eventual culminates into the release of the promoter contacts and the transition into elongation
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