5VE9
Structure of hACF7 EF1-EF2-GAR domains
Summary for 5VE9
Entry DOI | 10.2210/pdb5ve9/pdb |
Descriptor | Microtubule-actin cross-linking factor 1, isoforms 1/2/3/5, CALCIUM ION, ZINC ION, ... (5 entities in total) |
Functional Keywords | spectraplakin, ef-hand, microtubule binding, gas2, protein binding |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 3 |
Total formula weight | 30454.58 |
Authors | Lane, T.R.,Slep, K.C. (deposition date: 2017-04-04, release date: 2017-06-21, Last modification date: 2024-03-06) |
Primary citation | Lane, T.R.,Fuchs, E.,Slep, K.C. Structure of the ACF7 EF-Hand-GAR Module and Delineation of Microtubule Binding Determinants. Structure, 25:1130-1138.e6, 2017 Cited by PubMed Abstract: Spectraplakins are large molecules that cross-link F-actin and microtubules (MTs). Mutations in spectraplakins yield defective cell polarization, aberrant focal adhesion dynamics, and dystonia. We present the 2.8 Å crystal structure of the hACF7 EF1-EF2-GAR MT-binding module and delineate the GAR residues critical for MT binding. The EF1-EF2 and GAR domains are autonomous domains connected by a flexible linker. The EF1-EF2 domain is an EFβ-scaffold with two bound Ca ions that straddle an N-terminal α helix. The GAR domain has a unique α/β sandwich fold that coordinates Zn. While the EF1-EF2 domain is not sufficient for MT binding, the GAR domain is and likely enhances EF1-EF2-MT engagement. Residues in a conserved basic patch, distal to the GAR domain's Zn-binding site, mediate MT binding. PubMed: 28602822DOI: 10.1016/j.str.2017.05.006 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.795 Å) |
Structure validation
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