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Crystals of the Arp2/3 complex in two new space groups with structural information about actin‐related protein 2 and potential WASP binding sites
Author(s) -
Jurgenson Christopher T.,
Pollard Thomas D.
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x15013515
Subject(s) - actin , actin binding protein , space (punctuation) , microbiology and biotechnology , chemistry , biophysics , computational biology , biology , computer science , actin cytoskeleton , biochemistry , cytoskeleton , cell , operating system
Co‐crystals of the bovine Arp2/3 complex with the CA motif from N‐WASP in two new space groups were analyzed by X‐ray diffraction. The crystals in the orthorhombic space group P 2 1 2 1 2 1 contained one complex per asymmetric unit, with unit‐cell parameters a = 105.48, b = 156.71, c = 177.84 Å, and diffracted to 3.9 Å resolution. The crystals in the tetragonal space group P 4 1 contained two complexes per asymmetric unit, with unit‐cell parameters a = b = 149.93, c = 265.91 Å, and diffracted to 5.0 Å resolution. The electron‐density maps of both new crystal forms had densities for small segments of subdomains 1 and 2 of Arp2. Both maps had density at the binding site on Arp3 for the C‐terminal EWE tripeptide from N‐WASP and a binding site proposed for the C motif of N‐WASP in the barbed‐end groove of Arp2. The map from the tetragonal crystal form had density near the barbed end of Arp3 that may correspond to the C helix of N‐WASP. The noise levels and the low resolution of the maps made the assignment of specific molecular structures for any of these CA peptides impossible.