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PDBsum entry 1ubc
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Recombination
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PDB id
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1ubc
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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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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Abstract
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The crystal structures of Mycobacterium smegmatis RecA (RecA(Ms)) and its
complexes with ADP, ATPgammaS, and dATP show that RecA(Ms) has an expanded
binding site like that in Mycobacterium tuberculosis RecA, although there are
small differences between the proteins in their modes of nucleotide binding.
Nucleotide binding is invariably accompanied by the movement of Gln 196, which
appears to provide the trigger for transmitting the effect of nucleotide binding
to the DNA-binding loops. These observations provide a framework for exploring
the known properties of the RecA proteins.
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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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