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PDBsum entry 2g88
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Recombination
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PDB id
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2g88
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References listed in PDB file
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Key reference
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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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Abstract
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RecA protein is a crucial and central component of the homologous recombination
and DNA repair machinery. Despite numerous studies on the protein, several
issues concerning its action, including the allosteric regulation mechanism have
remained unclear. Here we report, for the first time, a crystal structure of a
complex of Mycobacterium smegmatis RecA (MsRecA) with dATP, which exhibits a
fully ordered C-terminal domain, with a second dATP molecule bound to it. ATP
binding is an essential step for all activities of RecA, since it triggers the
formation of active nucleoprotein filaments. In the crystal filament, dATP at
the first site communicates with a dATP of the second site of an adjacent
subunit, through conserved residues, suggesting a new route for allosteric
regulation. In addition, subtle but definite changes observed in the orientation
of the nucleotide at the first site and in the positions of the segment
preceding loop L2 as well as in the segment 102-105 situated between the 2 nt,
all appear to be concerted and suggestive of a biological role for the second
bound nucleotide.
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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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