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PDBsum entry 4ppg
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PDB id:
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Hydrolase
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Title:
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Mycobacterium tuberculosis reca citrate bound low temperature structure iia-br
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Structure:
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Protein reca, 1st part, 2nd part. Chain: a. Synonym: recombinase a. Engineered: yes
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Source:
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Mycobacterium tuberculosis. Organism_taxid: 1773. Gene: mt2806, mtv002.02c, reca, rv2737c. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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3.00Å
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R-factor:
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0.189
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R-free:
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0.248
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Authors:
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A.V.Chandran,J.R.Prabu,N.K.Patil,K.Muniyappa,M.Vijayan
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Key ref:
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A.V.Chandran
et al.
(2015).
Structural studies on Mycobacterium tuberculosis RecA: molecular plasticity and interspecies variability.
J Biosci,
40,
13-30.
PubMed id:
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Date:
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27-Feb-14
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Release date:
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18-Mar-15
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PROCHECK
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Headers
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References
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P9WHJ3
(RECA_MYCTU) -
Protein RecA from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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Seq:
Struc:
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790 a.a.
311 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 75 residue positions (black
crosses)
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J Biosci
40:13-30
(2015)
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PubMed id:
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Structural studies on Mycobacterium tuberculosis RecA: molecular plasticity and interspecies variability.
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A.V.Chandran,
J.R.Prabu,
A.Nautiyal,
K.N.Patil,
K.Muniyappa,
M.Vijayan.
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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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Links
