2GK7

Structural and Functional insights into the human Upf1 helicase core

Summary for 2GK7

• Entry DOI: 10.2210/pdb2gk7/pdb
• Related: 2GJK 2GK6 2GK8
• Descriptor: Regulator of nonsense transcripts 1, PHOSPHATE ION (3 entities in total)
• Functional Keywords: upf1, helicase, nmd, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q92900
• Total number of polymer chains: 1
• Total formula weight: 70151.39

Authors

Cheng, Z.,Muhlrad, D.,Parker, R.,Song, H. (deposition date: 2006-03-31, release date: 2007-01-09, Last modification date: 2023-10-25)

Primary citation

Cheng, Z.,Muhlrad, D.,Lim, M.K.,Parker, R.,Song, H.
Structural and functional insights into the human Upf1 helicase core
Embo J., 26:253-264, 2007

PubMed Abstract: Nonsense-mediated mRNA decay (NMD) is an mRNA surveillance pathway that recognizes and degrades aberrant mRNAs containing premature stop codons. A critical protein in NMD is Upf1p, which belongs to the helicase super family 1 (SF1), and is thought to utilize the energy of ATP hydrolysis to promote transitions in the structure of RNA or RNA-protein complexes. The crystal structure of the catalytic core of human Upf1p determined in three states (phosphate-, AMPPNP- and ADP-bound forms) reveals an overall structure containing two RecA-like domains with two additional domains protruding from the N-terminal RecA-like domain. Structural comparison combined with mutational analysis identifies a likely single-stranded RNA (ssRNA)-binding channel, and a cycle of conformational change coupled to ATP binding and hydrolysis. These conformational changes alter the likely ssRNA-binding channel in a manner that can explain how ATP binding destabilizes ssRNA binding to Upf1p.

PubMed: 17159905
DOI: 10.1038/sj.emboj.7601464

Experimental method

X-RAY DIFFRACTION (2.8 Å)