 |
|
Title
|
|
The structure of the E. coli recA protein monomer and polymer.
|
|
|
Authors
|
|
R.M.Story,
I.T.Weber,
T.A.Steitz.
|
|
|
Ref.
|
|
Nature, 1992,
355,
318-325.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The crystal structure of the recA protein from Escherichia coli at 2.3-A
resolution reveals a major domain that binds ADP and probably single- and
double-stranded DNA. Two smaller subdomains at the N and C termini protrude from
the protein and respectively stabilize a 6(1) helical polymer of protein
subunits and interpolymer bundles. This polymer structure closely resembles that
of recA/DNA filaments determined by electron microscopy. Mutations in recA
protein that enhance coprotease, DNA-binding and/or strand-exchange activity can
be explained if the interpolymer interactions in the crystal reflect a
regulatory mechanism in vivo.
|
|
|
|