1ku3

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|ACTIVITY=
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|RELATEDENTRY=[[1ku2|1KU2]], [[1ku7|1KU7]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ku3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ku3 OCA], [http://www.ebi.ac.uk/pdbsum/1ku3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ku3 RCSB]</span>
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[[Category: helix-turn-helix]]
[[Category: helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:53:38 2008''

Revision as of 18:53, 30 March 2008


PDB ID 1ku3

Drag the structure with the mouse to rotate
, resolution 1.8Å
Related: 1KU2, 1KU7


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Thermus aquaticus RNA Polymerase Sigma Subunit Fragment, Region 4


Overview

The sigma subunit is the key regulator of bacterial transcription. Proteolysis of Thermus aquaticus sigma(A), which occurred in situ during crystallization, reveals three domains, sigma(2), sigma(3), and sigma(4), connected by flexible linkers. Crystal structures of each domain were determined, as well as of sigma(4) complexed with -35 element DNA. Exposed surfaces of each domain are important for RNA polymerase binding. Universally conserved residues important for -10 element recognition and melting lie on one face of sigma(2), while residues important for extended -10 recognition lie on sigma(3). Genetic studies correctly predicted that a helix-turn-helix motif in sigma(4) recognizes the -35 element but not the details of the protein-DNA interactions. Positive control mutants in sigma(4) cluster in two regions, positioned to interact with activators bound just upstream or downstream of the -35 element.

About this Structure

1KU3 is a Single protein structure of sequence from Thermus aquaticus. Full crystallographic information is available from OCA.

Reference

Structure of the bacterial RNA polymerase promoter specificity sigma subunit., Campbell EA, Muzzin O, Chlenov M, Sun JL, Olson CA, Weinman O, Trester-Zedlitz ML, Darst SA, Mol Cell. 2002 Mar;9(3):527-39. PMID:11931761

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