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PDBsum entry 4po1
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DNA binding protein
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PDB id
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4po1
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References listed in PDB file
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Key reference
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Title
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Structural studies on mycobacterium tuberculosis reca: molecular plasticity and interspecies variability.
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Authors
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A.V.Chandran,
J.R.Prabu,
A.Nautiyal,
K.N.Patil,
K.Muniyappa,
M.Vijayan.
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Ref.
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J Biosci, 2015,
40,
13-30.
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PubMed id
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Abstract
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Structures of crystals of Mycobacterium tuberculosis RecA, grown and analysed
under different conditions, provide insights into hitherto underappreciated
details of molecular structure and plasticity. In particular, they yield
information on the invariant and variable features of the geometry of the
P-loop, whose binding to ATP is central for all the biochemical activities of
RecA. The strengths of interaction of the ligands with the P-loop reveal
significant differences. This in turn affects the magnitude of the motion of the
'switch' residue, Gln195 in M. tuberculosis RecA, which triggers the
transmission of ATP-mediated allosteric information to the DNA binding region.
M. tuberculosis RecA is substantially rigid compared with its counterparts from
M. smegmatis and E. coli, which exhibit concerted internal molecular mobility.
The interspecies variability in the plasticity of the two mycobacterial proteins
is particularly surprising as they have similar sequence and 3D structure.
Details of the interactions of ligands with the protein, characterized in the
structures reported here, could be useful for design of inhibitors against M.
tuberculosis RecA.
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Secondary reference #1
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Title
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Functionally important movements in reca molecules and filaments: studies involving mutation and environmental changes.
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Authors
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J.R.Prabu,
G.P.Manjunath,
N.R.Chandra,
K.Muniyappa,
M.Vijayan.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2008,
64,
1146-1157.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3 Snapshots in the trajectory of transformation from
form I to form IV. See text for details.
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Figure 7.
Figure 7 The position of the N-domain with respect to the rest
of the molecule in `inactive' (green) and `active' (magenta)
filaments.
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The above figures are
reproduced from the cited reference
with permission from the IUCr
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Secondary reference #2
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Title
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Crystallographic identification of an ordered c-Terminal domain and a second nucleotide-Binding site in reca: new insights into allostery.
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Authors
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R.Krishna,
G.P.Manjunath,
P.Kumar,
A.Surolia,
N.R.Chandra,
K.Muniyappa,
M.Vijayan.
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Ref.
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Nucleic Acids Res, 2006,
34,
2186-2195.
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PubMed id
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Secondary reference #3
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Title
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Crystal structures of mycobacterium smegmatis reca and its nucleotide complexes.
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Authors
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S.Datta,
R.Krishna,
N.Ganesh,
N.R.Chandra,
K.Muniyappa,
M.Vijayan.
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Ref.
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J Bacteriol, 2003,
185,
4280-4284.
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PubMed id
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Secondary reference #4
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Title
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Structural studies on mtreca-Nucleotide complexes: insights into DNA and nucleotide binding and the structural signature of ntp recognition.
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Authors
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S.Datta,
N.Ganesh,
N.R.Chandra,
K.Muniyappa,
M.Vijayan.
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Ref.
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Proteins, 2003,
50,
474-485.
[DOI no: ]
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PubMed id
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Figure 2.
Figure 2. A: A view down the axis of the MtRecA filament
highlighting the residues in the two loops, L1 and L2, that form
part of the inner core of the filament. DNA is expected to bind
at the groove in the centre. Superposition of the residues
corresponding to the loop (and five residues preceeding and five
residues succeding the loop) regions (B) L1 and (C) L2, L1 seen
clearly in the ATP  SMg^+2
complex and L2 seen in ATP S
complex, are shown in black. The loops in the other structures
were only partially decipherable from their electron density
maps, and are shown in gray shades.
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Figure 5.
Figure 5. Superposition of the core of the M domain (residues
38 to 239) (dark line) and the corresponding regions in the 13
structural neighbours (thin lines). Several residues are
numbered.
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The above figures are
reproduced from the cited reference
with permission from John Wiley & Sons, Inc.
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Secondary reference #5
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Title
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Crystal structures of mycobacterium tuberculosis reca and its complex with ADP-Alf(4): implications for decreased atpase activity and molecular aggregation.
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Authors
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S.Datta,
M.M.Prabu,
M.B.Vaze,
N.Ganesh,
N.R.Chandra,
K.Muniyappa,
M.Vijayan.
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Ref.
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Nucleic Acids Res, 2000,
28,
4964-4973.
[DOI no: ]
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PubMed id
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