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DNA binding protein
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PDB id
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2ewt
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Contents |
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* Residue conservation analysis
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PDB id:
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DNA binding protein
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Title:
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Crystal structure of the DNA-binding domain of bldd
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Structure:
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Putative DNA-binding protein. Chain: a. Fragment: DNA-binding domain. Synonym: bldd. Engineered: yes
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Source:
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Streptomyces coelicolor. Organism_taxid: 100226. Strain: a3(2). Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
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Resolution:
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1.81Å
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R-factor:
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0.188
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R-free:
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0.225
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Authors:
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I.K.Kim,C.J.Lee,M.K.Kim,J.M.Kim,J.H.Kim,H.S.Yim,S.S.Cha,S.O.
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Key ref:
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I.K.Kim
et al.
(2006).
Crystal structure of the DNA-binding domain of BldD, a central regulator of aerial mycelium formation in Streptomyces coelicolor A3(2).
Mol Microbiol,
60,
1179-1193.
PubMed id:
DOI:
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Date:
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07-Nov-05
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Release date:
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13-Jun-06
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PROCHECK
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Headers
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References
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O52732
(O52732_STRCO) -
Putative DNA binding protein
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Seq:
Struc:
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167 a.a.
71 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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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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2 terms
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DOI no:
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Mol Microbiol
60:1179-1193
(2006)
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PubMed id:
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Crystal structure of the DNA-binding domain of BldD, a central regulator of aerial mycelium formation in Streptomyces coelicolor A3(2).
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I.K.Kim,
C.J.Lee,
M.K.Kim,
J.M.Kim,
J.H.Kim,
H.S.Yim,
S.S.Cha,
S.O.Kang.
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ABSTRACT
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BldD is a central regulator of the developmental process in Streptomyces
coelicolor. The 1.8 angstroms resolution structure of the DNA-binding domain of
BldD (BldDN) reveals that BldDN forms a compact globular domain composed of four
helices (alpha1-alpha4) containing a helix-turn-helix motif (alpha2-alpha3)
resembling that of the DNA-binding domain of lambda repressor. The BldDN/DNA
complex model led us to design a series of mutants, which revealed the important
role of alpha3 and the 'turn' region between alpha2 and alpha3 for DNA
recognition. Based on the fact that BldD occupies two operator sites of bldN and
whiG and shows significant disparity in the affinity toward the two operator
sites when they are disconnected, we propose a model of cooperative binding,
which means that the binding of one BldD dimer to the high affinity site
facilitates that of the second BldD dimer to the low affinity site. In addition,
structural and mutational investigation reveals that the Tyr62Cys mutation,
found in the first-identified bldD mutant, can destabilize BldD structure by
disrupting the hydrophobic core.
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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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C.D.den Hengst,
N.T.Tran,
M.J.Bibb,
G.Chandra,
B.K.Leskiw,
and
M.J.Buttner
(2010).
Genes essential for morphological development and antibiotic production in Streptomyces coelicolor are targets of BldD during vegetative growth.
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Mol Microbiol, 78,
361-379.
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C.Chng,
A.M.Lum,
J.A.Vroom,
and
C.M.Kao
(2008).
A key developmental regulator controls the synthesis of the antibiotic erythromycin in Saccharopolyspora erythraea.
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Proc Natl Acad Sci U S A, 105,
11346-11351.
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C.J.Lee,
H.S.Won,
J.M.Kim,
B.J.Lee,
and
S.O.Kang
(2007).
Molecular domain organization of BldD, an essential transcriptional regulator for developmental process of Streptomyces coelicolor A3(2).
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Proteins, 68,
344-352.
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S.H.Chan,
Y.Bao,
E.Ciszak,
S.Laget,
and
S.Y.Xu
(2007).
Catalytic domain of restriction endonuclease BmrI as a cleavage module for engineering endonucleases with novel substrate specificities.
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Nucleic Acids Res, 35,
6238-6248.
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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.
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Links
