5jrj

Crystal Structure of Herbaspirillum seropedicae RecA

spinqualitylabelsall models 5jrj, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jrj is a 1 chain structure with sequence from Herbaspirillum seropedicae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: ADP, ATP, CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D8IYL4_HERSS Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage.[ARBA:ARBA00025580][HAMAP-Rule:MF_00268] Publication Abstract from PubMed The bacterial RecA protein plays a role in the complex system of DNA damage repair. Here, we report the functional and structural characterization of the Herbaspirillum seropedicae RecA protein (HsRecA). HsRecA protein is more efficient at displacing SSB protein from ssDNA than Escherichia coli RecA protein. HsRecA also promotes DNA strand exchange more efficiently. The three dimensional structure of HsRecA-ADP/ATP complex has been solved to 1.7 A resolution. HsRecA protein contains a small N-terminal domain, a central core ATPase domain and a large C-terminal domain, that are similar to homologous bacterial RecA proteins. Comparative structural analysis showed that the N-terminal polymerization motif of archaeal and eukaryotic RecA family proteins are also present in bacterial RecAs. Reconstruction of electrostatic potential from the hexameric structure of HsRecA-ADP/ATP revealed a high positive charge along the inner side, where ssDNA is bound inside the filament. The properties of this surface may explain the greater capacity of HsRecA protein to bind ssDNA, forming a contiguous nucleoprotein filament, displace SSB and promote DNA exchange relative to EcRecA. Our functional and structural analyses provide insight into the molecular mechanisms of polymerization of bacterial RecA as a helical nucleoprotein filament. Structural and Functional Studies of H. seropedicae RecA Protein - Insights into the Polymerization of RecA Protein as Nucleoprotein Filament.,Leite WC, Galvao CW, Saab SC, Iulek J, Etto RM, Steffens MB, Chitteni-Pattu S, Stanage T, Keck JL, Cox MM PLoS One. 2016 Jul 22;11(7):e0159871. doi: 10.1371/journal.pone.0159871., eCollection 2016. PMID:27447485 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also 3D structures of recombinase A

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