1gdr | pdb_00001gdr
MODEL FOR A DNA MEDIATED SYNAPTIC COMPLEX SUGGESTED BY CRYSTAL PACKING OF GAMMA DELTA RESOLVASE SUBUNITS
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Overview
The packing arrangement of the 12 subunits of intact gamma delta resolvase, in the unit cell of a hexagonal crystal form suggests a model for, site-specific recombination that involves a DNA-mediated synaptic, intermediate. The crystal structure has been determined by molecular, replacement and partially refined at 2.8/3.5 A resolution. Although the, small DNA-binding domain is disordered in these crystals, packing, considerations show that only a small region of space in the crystal could, accommodate a domain of its size. A family of related models for a, synaptic complex between two DNA duplexes and 12 monomers that are, arranged as situated in the crystal is consistent with the known topology, of the complex and the distances between the three resolvase dimer-binding, sites per DNA; further, these models place the two DNA recombination sites, in contact with each other between two resolvase dimers, implying that, strand exchange is accomplished through direct DNA-DNA interaction. A, major role postulated, then, for the resolvase protein assembly is to, stabilize a res DNA structure that is close to the topological transition, state of the reaction.
About this Structure
1GDR is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Model for a DNA-mediated synaptic complex suggested by crystal packing of gamma delta resolvase subunits., Rice PA, Steitz TA, EMBO J. 1994 Apr 1;13(7):1514-24. PMID:8156989
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