2NP2
Hbb-DNA complex
Summary for 2NP2
| Entry DOI | 10.2210/pdb2np2/pdb |
| Related | 1B8Z 1IHF 1OWF 1P51 1P71 1P78 |
| Descriptor | 36-MER, Hbb (3 entities in total) |
| Functional Keywords | protein-dna complex, dna-binding protein, dna-bending protein, dnabii family, hu/ihf family, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Borrelia burgdorferi (Lyme disease spirochete) |
| Total number of polymer chains | 4 |
| Total formula weight | 47513.85 |
| Authors | Rice, P.A.,Mouw, K.W. (deposition date: 2006-10-26, release date: 2007-02-27, Last modification date: 2023-08-30) |
| Primary citation | Mouw, K.W.,Rice, P.A. Shaping the Borrelia burgdorferi genome: crystal structure and binding properties of the DNA-bending protein Hbb. Mol.Microbiol., 63:1319-1330, 2007 Cited by PubMed Abstract: 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. PubMed: 17244195DOI: 10.1111/j.1365-2958.2007.05586.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.02 Å) |
Structure validation
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