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PDBsum entry 2ofo
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Recombination
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PDB id
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2ofo
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References listed in PDB file
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Key reference
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Title
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Snapshots of reca protein involving movement of the c-Domain and different conformations of the DNA-Binding loops: crystallographic and comparative analysis of 11 structures of mycobacterium smegmatis reca.
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Authors
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R.Krishna,
J.R.Prabu,
G.P.Manjunath,
S.Datta,
N.R.Chandra,
K.Muniyappa,
M.Vijayan.
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Ref.
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J Mol Biol, 2007,
367,
1130-1144.
[DOI no: ]
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PubMed id
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Abstract
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Mycobacterium smegmatis RecA and its nucleotide complexes crystallize in three
different, but closely related, forms characterized by specific ranges of unit
cell dimensions. The six crystals reported here and five reported earlier, all
grown under the same or very similar conditions, belong to these three forms,
all in space group P6(1). They include one obtained by reducing relative
humidity around the crystal. In all crystals, RecA monomers form filaments
around a 6(1) screw axis. Thus, the c-dimension of the crystal corresponds to
the pitch of the RecA filament. As reported for Escherichia coli RecA, the
variation in the pitch among the three forms correlates well with the motion of
the C-terminal domain of the RecA monomers with respect to the main domain. The
domain motion is compatible with formation of inactive as well as active RecA
filaments involving monomers with a fully ordered C domain. It does not appear
to influence the movement upon nucleotide-binding of the switch residue, which
is believed to provide the trigger for transmitting the effect of nucleotide
binding to the DNA-binding region. Interestingly, partial dehydration of the
crystal results in the movement of the residue similar to that caused by
nucleotide binding. The ordering of the DNA-binding loops, which present
ensembles of conformations, is also unaffected by domain motion. The
conformation of loop L2 appears to depend upon nucleotide binding, presumably on
account of the movement of the switch residue that forms part of the loop. The
conformations of loops L1 and L2 are correlated and have implications for
intermolecular communications within the RecA filament. The structures resulting
from different orientations of the C domain and different conformations of the
DNA-binding loops appear to represent snapshots of the RecA at different phases
of activity, and provide insights into the mechanism of action of RecA.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
367,
1130-1144)
copyright 2007.
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Secondary reference #1
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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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Secondary reference #2
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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 #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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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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