2np2: Difference between revisions
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|PDB= 2np2 |SIZE=350|CAPTION= <scene name='initialview01'>2np2</scene>, resolution 3.02Å | |PDB= 2np2 |SIZE=350|CAPTION= <scene name='initialview01'>2np2</scene>, resolution 3.02Å | ||
|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= hbb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi]) | |GENE= hbb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=139 Borrelia burgdorferi]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ihf|1IHF]], [[1p78|1P78]], [[1p71|1P71]], [[1p51|1P51]], [[1b8z|1B8Z]], [[1owf|1OWF]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2np2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2np2 OCA], [http://www.ebi.ac.uk/pdbsum/2np2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2np2 RCSB]</span> | |||
}} | }} | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:06:18 2008'' | ||
Revision as of 04:06, 31 March 2008
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| , resolution 3.02Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | hbb (Borrelia burgdorferi) | ||||||
| Related: | 1IHF, 1P78, 1P71, 1P51, 1B8Z, 1OWF
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Hbb-DNA complex
OverviewOverview
The genome of the Lyme disease-causing spirochete Borrelia burgdorferi encodes only a single polypeptide from the integration host factor (IHF)/HU or 'DNABII' family of nucleoid-associated proteins - Hbb. DNABII proteins induce large bends in DNA and serve as architectural factors in a variety of prokaryotic cellular processes. We have solved the crystal structure of an Hbb-DNA complex in which the DNA is bent by over 180 degrees . We find that like IHF, Hbb relies exclusively on indirect readout to recognize its cognate site. Additional binding studies show that the sequence preferences of Hbb are related to, yet distinct from those of IHF. Defining these binding characteristics may help to uncover additional roles for Hbb in Borrelia DNA metabolism as well as further our understanding of the mechanism of indirect readout.
About this StructureAbout this Structure
2NP2 is a Single protein structure of sequence from Borrelia burgdorferi. Full crystallographic information is available from OCA.
ReferenceReference
Shaping the Borrelia burgdorferi genome: crystal structure and binding properties of the DNA-bending protein Hbb., Mouw KW, Rice PA, Mol Microbiol. 2007 Mar;63(5):1319-30. Epub 2007 Jan 22. PMID:17244195
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