8DGL image
Deposition Date 2022-06-24
Release Date 2022-10-05
Last Version Date 2024-04-03
Entry Detail
PDB ID:
8DGL
Title:
Crystal Structure of the RdfS Excisionase
Biological Source:
Source Organism(s):
Expression System(s):
Method Details:
Experimental Method:
Resolution:
2.45 Å
R-Value Free:
0.24
R-Value Work:
0.19
R-Value Observed:
0.20
Space Group:
P 21 21 21
Macromolecular Entities
Structures with similar UniProt ID
Protein Blast
Polymer Type:polypeptide(L)
Molecule:Recombination Directionality
Gene (Uniprot):msi109
Chain IDs:A, B, C, D
Chain Length:91
Number of Molecules:4
Biological Source:Mesorhizobium japonicum R7A
Primary Citation
Crystallographic and X-ray scattering study of RdfS, a recombination directionality factor from an integrative and conjugative element.
Acta Crystallogr D Struct Biol 78 1210 1220 (2022)
PMID: 36189741 DOI: 10.1107/S2059798322008579

Abstact

The recombination directionality factors from Mesorhizobium spp. (RdfS) are involved in regulating the excision and transfer of integrative and conjugative elements. Here, solution small-angle X-ray scattering, and crystallization and preliminary structure solution of RdfS from Mesorhizobium japonicum R7A are presented. RdfS crystallizes in space group P212121, with evidence of eightfold rotational crystallographic/noncrystallographic symmetry. Initial structure determination by molecular replacement using ab initio models yielded a partial model (three molecules), which was completed after manual inspection revealed unmodelled electron density. The finalized crystal structure of RdfS reveals a head-to-tail polymer forming left-handed superhelices with large solvent channels. Additionally, RdfS has significant disorder in the C-terminal region of the protein, which is supported by the solution scattering data and the crystal structure. The steps taken to finalize structure determination, as well as the scattering and crystallographic characteristics of RdfS, are discussed.

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