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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 single-stranded DNA-binding protein from mycobacterium smegmatis
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Structure:
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Single-strand binding protein. Chain: a, b. Synonym: single-stranded DNA-binding protein, ssb, helix- destabilizing protein. Engineered: yes
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Source:
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Mycobacterium smegmatis. Organism_taxid: 1772. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Tetramer (from PDB file)
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Resolution:
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2.15Å
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R-factor:
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0.202
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R-free:
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0.239
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Authors:
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K.Saikrishnan,G.P.Manjunath,P.Singh,J.Jeyakanthan,Z.Dauter,K.Sekar, K.Muniyappa,M.Vijayan
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Key ref:
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K.Saikrishnan
et al.
(2005).
Structure of Mycobacterium smegmatis single-stranded DNA-binding protein and a comparative study involving homologus SSBs: biological implications of structural plasticity and variability in quaternary association.
Acta Crystallogr D Biol Crystallogr,
61,
1140-1148.
PubMed id:
DOI:
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Date:
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04-May-05
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Release date:
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15-Aug-05
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B:
E.C.?
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DOI no:
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Acta Crystallogr D Biol Crystallogr
61:1140-1148
(2005)
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PubMed id:
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Structure of Mycobacterium smegmatis single-stranded DNA-binding protein and a comparative study involving homologus SSBs: biological implications of structural plasticity and variability in quaternary association.
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K.Saikrishnan,
G.P.Manjunath,
P.Singh,
J.Jeyakanthan,
Z.Dauter,
K.Sekar,
K.Muniyappa,
M.Vijayan.
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ABSTRACT
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The structure of Mycobacterium smegmatis single-stranded DNA-binding protein
(SSB) has been determined using three data sets collected from related crystals.
The structure is similar to that of its homologue from Mycobacterium
tuberculosis, indicating that the clamp arrangement that stabilizes the dimer
and the ellipsoidal shape of the tetramer are characteristic features of
mycobacterial SSBs. The central OB fold is conserved in mycobacterial SSBs as
well as those from Escherichia coli, Deinococcus radiodurans and human
mitochondria. However, the quaternary structure exhibits considerable
variability. The observed plasticity of the subunit is related to this
variability. The crystal structures and modelling provide a rationale for the
variability. The strand involved in the clamp mechanism, which leads to higher
stability of the tetramer, appears to occur in all high-G+C Gram-positive
bacteria. The higher stability is perhaps required by these organisms. The mode
of DNA binding of mycobacterial SSBs is different from that of E. coli SSB
partly on account of the difference in the shape of the tetramers. Another
difference between the two modes is that the former contains additional ionic
interactions and is more susceptible to salt concentration.
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Selected figure(s)
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Figure 1.
Figure 1
A 2F[o] - F[c] omit map for the stretch of residues 102-120. The figure was generated
using BOBSCRIPT (Esnouf, 1997 [Esnouf, R. M. (1997). J. Mol. Graph. 15,
132-134.]-[bluearr.gif] ). The map was contoured at 1 [sigma] .
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Figure 6.
Figure 6
Surface diagram of MsSSB, DrSSB and EcSSB viewed down the twofold axis P (represented as a
blue ball), highlighting the variation in the orientation of the OB folds. Subunits A and
C of MsSSB and EcSSB and subunit A of DrSSB were superposed onto one another (represented
in grey) to bring out the difference in the orientation of subunits B and D of MsSSB
(magenta) and EcSSB (red) and subunit B of DrSSB (green). The loops are omitted for
clarity.
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2005,
61,
1140-1148)
copyright 2005.
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Figures were
selected
by an automated process.
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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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H.C.Jan,
Y.L.Lee,
and
C.Y.Huang
(2011).
Characterization of a Single-Stranded DNA-Binding Protein from Pseudomonas aeruginosa PAO1.
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Protein J,
30,
20-26.
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M.Wu,
Y.J.Park,
E.Pardon,
S.Turley,
A.Hayhurst,
J.Deng,
J.Steyaert,
and
W.G.Hol
(2011).
Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies.
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J Struct Biol,
174,
124-136.
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PDB codes:
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Y.H.Huang,
Y.L.Lee,
and
C.Y.Huang
(2011).
Characterization of a Single-Stranded DNA Binding Protein from Salmonella enterica Serovar Typhimurium LT2.
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Protein J,
30,
102-108.
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A.G.Kozlov,
J.M.Eggington,
M.M.Cox,
and
T.M.Lohman
(2010).
Binding of the dimeric Deinococcus radiodurans single-stranded DNA binding protein to single-stranded DNA.
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Biochemistry,
49,
8266-8275.
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P.S.Kaushal,
P.Singh,
A.Sharma,
K.Muniyappa,
and
M.Vijayan
(2010).
X-ray and molecular-dynamics studies on Mycobacterium leprae single-stranded DNA-binding protein and comparison with other eubacterial SSB structures.
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Acta Crystallogr D Biol Crystallogr,
66,
1048-1058.
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PDB codes:
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B.Marintcheva,
U.Qimron,
Y.Yu,
S.Tabor,
and
C.Richardson
(2009).
Mutations in the gene 5 DNA polymerase of bacteriophage T7 suppress the dominant lethal phenotype of gene 2.5 ssDNA binding protein lacking the C-terminal phenylalanine.
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Mol Microbiol,
72,
869-880.
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L.Shokri,
I.Rouzina,
and
M.C.Williams
(2009).
Interaction of bacteriophage T4 and T7 single-stranded DNA-binding proteins with DNA.
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Phys Biol,
6,
25002.
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B.Marintcheva,
A.Marintchev,
G.Wagner,
and
C.C.Richardson
(2008).
Acidic C-terminal tail of the ssDNA-binding protein of bacteriophage T7 and ssDNA compete for the same binding surface.
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Proc Natl Acad Sci U S A,
105,
1855-1860.
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D.Das,
H.Hyun,
Y.Lou,
H.Yokota,
R.Kim,
and
S.H.Kim
(2007).
Crystal structure of a novel single-stranded DNA binding protein from Mycoplasma pneumoniae.
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Proteins,
67,
776-782.
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PDB code:
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J.R.Prabu,
S.Thamotharan,
J.S.Khanduja,
E.Z.Alipio,
C.Y.Kim,
G.S.Waldo,
T.C.Terwilliger,
B.Segelke,
T.Lekin,
D.Toppani,
L.W.Hung,
M.Yu,
E.Bursey,
K.Muniyappa,
N.R.Chandra,
and
M.Vijayan
(2006).
Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
731-734.
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PDB code:
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R.Fedorov,
G.Witte,
C.Urbanke,
D.J.Manstein,
and
U.Curth
(2006).
3D structure of Thermus aquaticus single-stranded DNA-binding protein gives insight into the functioning of SSB proteins.
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Nucleic Acids Res,
34,
6708-6717.
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PDB codes:
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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
codes are
shown on the right.
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}
}
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