1r71
From Proteopedia
(New page: 200px<br /><applet load="1r71" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r71, resolution 2.20Å" /> '''Crystal Structure of...) |
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| - | [[Image:1r71.gif|left|200px]]<br /><applet load="1r71" size=" | + | [[Image:1r71.gif|left|200px]]<br /><applet load="1r71" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r71, resolution 2.20Å" /> | caption="1r71, resolution 2.20Å" /> | ||
'''Crystal Structure of the DNA binding domain of KorB in complex with the operator DNA'''<br /> | '''Crystal Structure of the DNA binding domain of KorB in complex with the operator DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The KorB protein of the broad-host-range plasmid RP4 acts as a | + | The KorB protein of the broad-host-range plasmid RP4 acts as a multifunctional regulator of plasmid housekeeping genes, including those responsible for replication, maintenance and conjugation. Additionally, KorB functions as the ParB analog of the plasmid's partitioning system. The protein structure consists of eight helices, two of which belong to a predicted helix-turn-helix motif. Each half-site of the palindromic operator DNA binds one copy of the protein in the major groove. As confirmed by mutagenesis, recognition specificity is based mainly on two side chain interactions outside the helix-turn-helix motif with two bases next to the central base pair of the 13-base pair operator sequence. The surface of the KorB DNA-binding domain mirrors the overall acidity of KorB, whereas DNA binding occurs via a basic interaction surface. We present a model of KorB, including the structure of its dimerization domain, and discuss its interactions with the highly basic ParA homolog IncC. |
==About this Structure== | ==About this Structure== | ||
| - | 1R71 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1R71 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R71 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:45 2008'' |
Revision as of 12:47, 21 February 2008
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Crystal Structure of the DNA binding domain of KorB in complex with the operator DNA
Overview
The KorB protein of the broad-host-range plasmid RP4 acts as a multifunctional regulator of plasmid housekeeping genes, including those responsible for replication, maintenance and conjugation. Additionally, KorB functions as the ParB analog of the plasmid's partitioning system. The protein structure consists of eight helices, two of which belong to a predicted helix-turn-helix motif. Each half-site of the palindromic operator DNA binds one copy of the protein in the major groove. As confirmed by mutagenesis, recognition specificity is based mainly on two side chain interactions outside the helix-turn-helix motif with two bases next to the central base pair of the 13-base pair operator sequence. The surface of the KorB DNA-binding domain mirrors the overall acidity of KorB, whereas DNA binding occurs via a basic interaction surface. We present a model of KorB, including the structure of its dimerization domain, and discuss its interactions with the highly basic ParA homolog IncC.
About this Structure
1R71 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Sequence-specific DNA binding determined by contacts outside the helix-turn-helix motif of the ParB homolog KorB., Khare D, Ziegelin G, Lanka E, Heinemann U, Nat Struct Mol Biol. 2004 Jul;11(7):656-63. Epub 2004 May 30. PMID:15170177
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