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5VE9

Structure of hACF7 EF1-EF2-GAR domains

Summary for 5VE9
Entry DOI10.2210/pdb5ve9/pdb
DescriptorMicrotubule-actin cross-linking factor 1, isoforms 1/2/3/5, CALCIUM ION, ZINC ION, ... (5 entities in total)
Functional Keywordsspectraplakin, ef-hand, microtubule binding, gas2, protein binding
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains3
Total formula weight30454.58
Authors
Lane, T.R.,Slep, K.C. (deposition date: 2017-04-04, release date: 2017-06-21, Last modification date: 2024-03-06)
Primary citationLane, 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: 28602822
DOI: 10.1016/j.str.2017.05.006
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.795 Å)
Structure validation

239803

数据于2025-08-06公开中

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