4U0U: Wild Type Eukaryotic Fic Domain Containing Protein With Adp

Citation:
Abstract
Protein AMPylation, the transfer of AMP from ATP to protein targets, has been recognized as a new mechanism of host-cell disruption by some bacterial effectors that typically contain a FIC-domain. Eukaryotic genomes also encode one FIC-domain protein,HYPE, which has remained poorly characterized.Here we describe the structure of human HYPE, solved by X-ray crystallography, representing the first structure of a eukaryotic FIC-domain protein. We demonstrate that HYPE forms stable dimers with structurally and functionally integrated FIC-domains and with TPR-motifs exposed for protein-protein interactions. As HYPE also uniquely possesses a transmembrane helix, dimerization is likely to affect its positioning and function in the membrane vicinity. The low rate of auto AMPylation of the wild-type HYPE could be due to autoinhibition, consistent with the mechanism proposed for a number of putative FIC AMPylators. Our findings also provide a basis to further consider possible alternative cofactors of HYPE and distinct modes of target-recognition.
PDB ID: 4U0UDownload
MMDB ID: 125482
PDB Deposition Date: 2014/7/14
Updated in MMDB: 2014/12
Experimental Method:
x-ray diffraction
Resolution: 2.98  Å
Source Organism:
Similar Structures:
Biological Unit for 4U0U: dimeric; determined by author and by software (PISA)
Molecular Components in 4U0U
Label Count Molecule
Proteins (2 molecules)
2
Adenosine Monophosphate-protein Transferase Ficd(Gene symbol: FICD)
Molecule annotation
Chemicals (7 molecules)
1
3
2
2
3
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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