4XXO: Crystal Structure Of Human Apobec3a

Citation:
Abstract
Deaminase activity mediated by the human APOBEC3 family of proteins contributes to genomic instability and cancer. APOBEC3A is by far the most active in this family and can cause rapid cell death when overexpressed, but in general how the activity of APOBEC3s is regulated on a molecular level is unclear. In this study, the biochemical and structural basis of APOBEC3A substrate binding and specificity is elucidated. We find that specific binding of single-stranded DNA is regulated by the cooperative dimerization of APOBEC3A. The crystal structure elucidates this homodimer as a symmetric domain swap of the N-terminal residues. This dimer interface provides insights into how cooperative protein-protein interactions may affect function in the APOBEC3 enzymes and provides a potential scaffold for strategies aimed at reducing their mutation load.
PDB ID: 4XXODownload
MMDB ID: 128921
PDB Deposition Date: 2015/1/30
Updated in MMDB: 2017/10
Experimental Method:
x-ray diffraction
Resolution: 2.84  Å
Source Organism:
Similar Structures:
Biological Unit for 4XXO: dimeric; determined by author and by software (PISA)
Molecular Components in 4XXO
Label Count Molecule
Proteins (2 molecules)
2
DNA Dc->du-editing Enzyme Apobec-3a(Gene symbol: APOBEC3A)
Molecule annotation
Chemicals (9 molecules)
1
7
2
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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