4XEI
Orthorhombic isomorph of bovine Arp2/3 complex
Summary for 4XEI
Entry DOI | 10.2210/pdb4xei/pdb |
Descriptor | Actin-related protein 3, Actin-related protein 2, Actin-related protein 2/3 complex subunit 1B, ... (8 entities in total) |
Functional Keywords | structural protein |
Biological source | Bos taurus (Bovine) More |
Cellular location | Cytoplasm, cytoskeleton : P61157 A7MB62 Q58CQ2 Q3MHR7 Q3T035 Q148J6 Q3SYX9 |
Total number of polymer chains | 7 |
Total formula weight | 224230.55 |
Authors | Jurgenson, C.J.,Pollard, T.P. (deposition date: 2014-12-23, release date: 2015-09-02, Last modification date: 2024-10-30) |
Primary citation | Jurgenson, C.T.,Pollard, T.D. Crystals of the Arp2/3 complex in two new space groups with structural information about actin-related protein 2 and potential WASP binding sites. Acta Crystallogr.,Sect.F, 71:1161-1168, 2015 Cited by PubMed Abstract: 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 P212121 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 P41 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. PubMed: 26323303DOI: 10.1107/S2053230X15013515 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.874 Å) |
Structure validation
Download full validation report
