1I2T

X-RAY STRUCTURE OF THE HUMAN HYPERPLASTIC DISCS PROTEIN: AN ORTHOLOG OF THE C-TERMINAL DOMAIN OF POLY(A)-BINDING PROTEIN

Summary for 1I2T

• Entry DOI: 10.2210/pdb1i2t/pdb
• Descriptor: HYD PROTEIN (2 entities in total)
• Functional Keywords: four alpha-helical domain, ligase
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 6748.89

Authors

Deo, R.C.,Sonenberg, N.,Burley, S.K. (deposition date: 2001-02-12, release date: 2001-04-18, Last modification date: 2024-02-07)

Primary citation

Deo, R.C.,Sonenberg, N.,Burley, S.K.
X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein.
Proc.Natl.Acad.Sci.USA, 98:4414-4419, 2001

PubMed Abstract: The poly(A)-binding protein (PABP) recognizes the 3' mRNA poly(A) tail and plays an essential role in eukaryotic translation initiation and mRNA stabilization/degradation. PABP is a modular protein, with four N-terminal RNA-binding domains and an extensive C terminus. The C-terminal region of PABP is essential for normal growth in yeast and has been implicated in mediating PABP homo-oligomerization and protein-protein interactions. A small, proteolytically stable, highly conserved domain has been identified within this C-terminal segment. Remarkably, this domain is also present in the hyperplastic discs protein (HYD) family of ubiquitin ligases. To better understand the function of this conserved region, an x-ray structure of the PABP-like segment of the human HYD protein has been determined at 1.04-A resolution. The conserved domain adopts a novel fold resembling a right-handed supercoil of four alpha-helices. Sequence profile searches and comparative protein structure modeling identified a small ORF from the Arabidopsis thaliana genome that encodes a structurally similar but distantly related PABP/HYD domain. Phylogenetic analysis of the experimentally determined (HYD) and homology modeled (PABP) protein surfaces revealed a conserved feature that may be responsible for binding to a PABP interacting protein, Paip1, and other shared interaction partners.

PubMed: 11287654
DOI: 10.1073/pnas.071552198

Experimental method

X-RAY DIFFRACTION (1.04 Å)