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DNA binding protein/DNA
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PDB id
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2np2
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Contents |
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biochemical function
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DNA binding
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1 term
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DOI no:
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Mol Microbiol
63:1319-1330
(2007)
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PubMed id:
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Shaping the Borrelia burgdorferi genome: crystal structure and binding properties of the DNA-bending protein Hbb.
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K.W.Mouw,
P.A.Rice.
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ABSTRACT
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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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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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M.Firczuk,
M.Wojciechowski,
H.Czapinska,
and
M.Bochtler
(2011).
DNA intercalation without flipping in the specific ThaI-DNA complex.
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Nucleic Acids Res, 39,
744-754.
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PDB code:
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M.S.Medrano,
P.F.Policastro,
T.G.Schwan,
and
J.Coburn
(2010).
Interaction of Borrelia burgdorferi Hbb with the p66 promoter.
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Nucleic Acids Res, 38,
414-427.
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A.R.Dresser,
P.O.Hardy,
and
G.Chaconas
(2009).
Investigation of the genes involved in antigenic switching at the vlsE locus in Borrelia burgdorferi: an essential role for the RuvAB branch migrase.
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PLoS Pathog, 5,
e1000680.
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S.P.Riley,
T.Bykowski,
A.E.Cooley,
L.H.Burns,
K.Babb,
C.A.Brissette,
A.Bowman,
M.Rotondi,
M.C.Miller,
E.DeMoll,
K.Lim,
M.G.Fried,
and
B.Stevenson
(2009).
Borrelia burgdorferi EbfC defines a newly-identified, widespread family of bacterial DNA-binding proteins.
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Nucleic Acids Res, 37,
1973-1983.
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T.J.Moriarty,
and
G.Chaconas
(2009).
Identification of the determinant conferring permissive substrate usage in the telomere resolvase, ResT.
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J Biol Chem, 284,
23293-23301.
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A.Mukherjee,
A.O.Sokunbi,
and
A.Grove
(2008).
DNA protection by histone-like protein HU from the hyperthermophilic eubacterium Thermotoga maritima.
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Nucleic Acids Res, 36,
3956-3968.
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X.Peng,
Y.Z.Pigli,
P.A.Rice,
and
M.M.Greenberg
(2008).
Protein binding has a large effect on radical mediated DNA damage.
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J Am Chem Soc, 130,
12890-12891.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
