2016
DOI: 10.1021/acs.biochem.5b01383
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Molecular Mechanism Underlying ATP-Induced Conformational Changes in the Nucleoprotein Filament of Mycobacterium smegmatis RecA

Abstract: RecA plays a central role in bacterial DNA repair, homologous recombination, and restoration of stalled replication forks by virtue of its active extended nucleoprotein filament. Binding of ATP and its subsequent recognition by the carboxamide group of a highly conserved glutamine (Gln196 in MsRecA) have been implicated in the formation of active RecA nucleoprotein filaments. Although the mechanism of ATP-dependent structural transitions in RecA has been proposed on the basis of low-resolution electron microsc… Show more

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Cited by 10 publications
(7 citation statements)
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“…The crystal structure of a complex of MsRecA with dATP revealed the presence of a second dATP molecule bound to it within the fully ordered C‐terminal domain (Krishna et al, ). However, conformation of the second dATP is different from that of the first dATP molecule; also, the primary (but not the secondary) dATP site in MsRecA isomerizes into the ATP binding pocket in the active nucleoprotein filament (Manjunath et al, ). Based on the data presented here, we infer that the presence of dATP in the MsRecA crystal was incidental and that cyclic di‐AMP is the natural ligand for the second nucleotide binding site embedded in the C‐terminus of MsRecA.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…The crystal structure of a complex of MsRecA with dATP revealed the presence of a second dATP molecule bound to it within the fully ordered C‐terminal domain (Krishna et al, ). However, conformation of the second dATP is different from that of the first dATP molecule; also, the primary (but not the secondary) dATP site in MsRecA isomerizes into the ATP binding pocket in the active nucleoprotein filament (Manjunath et al, ). Based on the data presented here, we infer that the presence of dATP in the MsRecA crystal was incidental and that cyclic di‐AMP is the natural ligand for the second nucleotide binding site embedded in the C‐terminus of MsRecA.…”
Section: Discussionmentioning
confidence: 99%
“…However, conformation of the second dATP was different from that of the first dATP molecule (which binds at the N-terminal region in the P-loop), suggesting a regulatory role for the nucleotide bound at the second site. Furthermore, the primary (but not the secondary) nucleotide binding site in MsRecA isomerizes into the ATP binding site in the active RecA nucleoprotein filament (Manjunath et al, 2016). The multiple sequence alignment of RecA amino acid sequences of MtRecA and MsRecA with EcRecA reveals significant sequence divergence among these proteins at their C-terminus ( Fig.…”
Section: Identification Of Reca As Cyclic Di-amp Binding Proteinmentioning
confidence: 97%
“…A homology model for the inactive counterpart of our structure for the active presynaptic RAD51 filament bound to the ATP analogue AMP-PNP (target) was constructed as per our previously reported approach (37) using the MODELLER version 9.14 suite of programmes (38,39). The structure of the E. Coli RecA in the inactive ADP-bound form (PDB: 1XMS, ref.…”
Section: Methodsmentioning
confidence: 99%
“…There is, however, no structural clue about a mechanism for such chemical to rotational energy transfer. The third hypothesis postulates that monomers switch their binding geometries in the filament from ATP- to ADP-favorable interfaces in response to ATP hydrolysis (24,31). They can then exchange the bound ADP for a new ATP and perform reverse interface switching, thus completing the ATP cycle.…”
Section: Introductionmentioning
confidence: 99%