1owg: Difference between revisions
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[[Image:1owg.gif|left|200px]] | [[Image:1owg.gif|left|200px]] | ||
'''Crystal structure of WT IHF complexed with an altered H' site (T44A)''' | {{Structure | ||
|PDB= 1owg |SIZE=350|CAPTION= <scene name='initialview01'>1owg</scene>, resolution 2.10Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''Crystal structure of WT IHF complexed with an altered H' site (T44A)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1OWG is a [ | 1OWG is a [[Protein complex]] structure of sequences 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=1OWG OCA]. | ||
==Reference== | ==Reference== | ||
Integration host factor: putting a twist on protein-DNA recognition., Lynch TW, Read EK, Mattis AN, Gardner JF, Rice PA, J Mol Biol. 2003 Jul 11;330(3):493-502. PMID:[http:// | Integration host factor: putting a twist on protein-DNA recognition., Lynch TW, Read EK, Mattis AN, Gardner JF, Rice PA, J Mol Biol. 2003 Jul 11;330(3):493-502. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12842466 12842466] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein-dna recognition]] | [[Category: protein-dna recognition]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:16:37 2008'' | ||
Revision as of 11:16, 20 March 2008
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| 1owg, resolution 2.10Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Crystal structure of WT IHF complexed with an altered H' site (T44A)
Overview
Integration host factor (IHF) is a DNA-bending protein that recognizes its cognate sites through indirect readout. Previous studies have shown that binding of wild-type (WT)-IHF is disrupted by a T to A mutation at the center position of a conserved TTR motif in its binding site, and that substitution of betaGlu44 with Ala prevented IHF from discriminating between A and T at this position. We have determined the crystal structures and relative binding affinities for all combinations of WT-IHF and IHF-betaGlu44Ala bound to the WT and mutant DNAs. Comparison of these structures reveals that DNA twist plays a major role in DNA recognition by IHF, and that this geometric parameter is dependent on the dinucleotide step and not on the bound IHF variant.
About this Structure
1OWG is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Integration host factor: putting a twist on protein-DNA recognition., Lynch TW, Read EK, Mattis AN, Gardner JF, Rice PA, J Mol Biol. 2003 Jul 11;330(3):493-502. PMID:12842466
Page seeded by OCA on Thu Mar 20 13:16:37 2008
