3ZUZ

Structure of Shq1p C-terminal domain

Summary for 3ZUZ

• Entry DOI: 10.2210/pdb3zuz/pdb
• Related: 3ZV0
• Descriptor: PROTEIN SHQ1, ISOPROPYL ALCOHOL (3 entities in total)
• Functional Keywords: cell cycle, rnp assembly, x-linked dyskeratosis congenita, telomerase
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Total number of polymer chains: 1
• Total formula weight: 43056.35

Authors

Walbott, H.,Machado-Pinilla, R.,Liger, D.,Blaud, M.,Rety, S.,Grozdanov, P.N.,Godin, K.,vanTilbeurgh, H.,Varani, G.,Meier, U.T.,Leulliot, N. (deposition date: 2011-07-22, release date: 2011-11-30, Last modification date: 2019-02-27)

Primary citation

Walbott, H.,Machado-Pinilla, R.,Liger, D.,Blaud, M.,Rety, S.,Grozdanov, P.N.,Godin, K.,Van Tilbeurgh, H.,Varani, G.,Meier, U.T.,Leulliot, N.
The H/Aca Rnp Assembly Factor Shq1 Functions as an RNA Mimic.
Genes Dev., 25:2398-, 2011

PubMed Abstract: SHQ1 is an essential assembly factor for H/ACA ribonucleoproteins (RNPs) required for ribosome biogenesis, pre-mRNA splicing, and telomere maintenance. SHQ1 binds dyskerin/NAP57, the catalytic subunit of human H/ACA RNPs, and this interaction is modulated by mutations causing X-linked dyskeratosis congenita. We report the crystal structure of the C-terminal domain of yeast SHQ1, Shq1p, and its complex with yeast dyskerin/NAP57, Cbf5p, lacking its catalytic domain. The C-terminal domain of Shq1p interacts with the RNA-binding domain of Cbf5p and, through structural mimicry, uses the RNA-protein-binding sites to achieve a specific protein-protein interface. We propose that Shq1p operates as a Cbf5p chaperone during RNP assembly by acting as an RNA placeholder, thereby preventing Cbf5p from nonspecific RNA binding before association with an H/ACA RNA and the other core RNP proteins.

PubMed: 22085966
DOI: 10.1101/GAD.176834.111

Experimental method

X-RAY DIFFRACTION (1.5 Å)