NDLI: Structural constraints on autoprocessing of the human nucleoporin Nup98.

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Structural constraints on autoprocessing of the human nucleoporin Nup98.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Sun, Yixin Guo, Hwai-Chen
Description	Country affiliation: United States Author Affiliation: Sun Y ( Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118-2526, USA.)
Abstract	Nucleoporin Nup98, a 98-kDa protein component of the nuclear pore complex, plays an important role in both protein and RNA transport. During its maturation process, Nup98 undergoes post-translational autoproteolysis, which is critical for targeting to the NPC. Here we present high-resolution crystal structures of the C-terminal autoproteolytic domains of Nup98 (2.3 A for the wild type and 1.9 A for the S864A precursor), and propose a detailed autoproteolysis mechanism through an N-O acyl shift. Structural constraints are found at the autocleavage site, and could thus provide a driving force for autocleavage at the scissile peptide bond. Such structural constraints appear to be generated, at least in part, by anchoring a conserved phenylalanine side chain into a highly conserved hydrophobic pocket at the catalytic site. Our high-resolution crystal structures also reveal that three highly conserved residues, Tyr866, Gly867, and Leu868, provide most of the interactions between the autoproteolytic domain and the C-terminal tail. These results suggest that Nup98 may represent a new subtype of protein that utilizes autoprocessing to control biogenesis pathways and intracellular translocation.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1110/ps.073311808
Journal	Protein Science
Issue Number	3
Volume Number	17
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2008-03-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Nuclear Pore Complex Proteins Chemistry Catalysis Crystallography, X-ray Hydrogen Bonding Models, Molecular Metabolism Protein Processing, Post-translational Protein Structure, Tertiary Research Support, N.i.h., Extramural Research Support, U.s. Gov't, Non-p.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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