ISDA: 2NP2

Deposition Date 2006-10-26

Release Date 2007-02-27

Last Version Date 2023-08-30

Entry Detail

PDB ID:

2NP2

Keywords:

DNA BINDING PROTEIN/DNA

Title:

Hbb-DNA complex

Biological Source:

Source Organism(s):

Borrelia burgdorferi (Taxon ID: 139)

Expression System(s):

Escherichia coli

Method Details:

Experimental Method:

X-RAY DIFFRACTION

Resolution:

3.02 Å

R-Value Free:

0.27

R-Value Work:

0.23

R-Value Observed:

0.23

Space Group:

P 21 21 21

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Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Hbb
Chain IDs:C (auth: A), D (auth: B)
Chain Length:108
Number of Molecules:2
Biological Source:Borrelia burgdorferi

UniProt ID:Q57267 Pfam ID:PF00216

Primary Citation

Shaping the Borrelia burgdorferi genome: crystal structure and binding properties of the DNA-bending protein Hbb.

Mouw, K.W, Rice, P.A.Show

Mol. Microbiol. 63 1319 1330 (2007)

PMID: 17244195 DOI: 10.1111/j.1365-2958.2007.05586.x

Abstact

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.

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