Structure of the guanine nucleotide exchange factor Sec7 domain of human Arno and analysis of the interaction with ARF GTPpase Journal Article

  

Authors:	Mossessova, E.; Gulbis, J. M.; Goldberg, J.
Article Title:	Structure of the guanine nucleotide exchange factor Sec7 domain of human Arno and analysis of the interaction with ARF GTPpase
Abstract:	Sac7-related guanine nucleotide exchange factors (GEFs) initiate vesicle budding from the Golgi membrane surface by converting the GTPase ARF to a GTPbound, membrane-associated form. Here we report the crystal structure of the catalytic Sac7 homology domain of Arno, a human GEF for ARF1, determined at 2.2 Å resolution. The Sac7 domain is an elongated, all-helical protein with a distinctive hydrophobic groove that is phylogenetically conserved. Structure-based mutagenesis identifies the groove and an adjacent conserved loop as the ARF-interacting surface. The sites of Sec7 domain interaction on ARF1 have subsequently been mapped, by protein footprinting experiments, to the switch 1 and switch 2 GTPase regions, leading to a model for the interaction between ARF GTPases and Sec7 domain exchange factors.
Keywords:	human cell; sequence analysis; sequence deletion; protein domain; protein protein interaction; gtp-binding proteins; amino acid sequence; molecular sequence data; sequence homology, amino acid; enzyme analysis; gtpase-activating proteins; crystallography, x-ray; mutagenesis, site-directed; protein structure, tertiary; binding sites; protein structure; sequence homology; gene switching; membrane binding; gtp phosphohydrolases; phylogeny; guanine nucleotide exchange factors; membrane vesicle; fungal proteins; guanosine diphosphate; guanine nucleotide exchange factor; guanosine triphosphatase; alpha helix; myristylation; hydrophobicity; dna footprinting; adp-ribosylation factor 1; adp-ribosylation factors; humans; human; priority journal; article
Journal Title:	Cell
Volume:	92
Issue:	3
ISSN:	0092-8674
Publisher:	Cell Press
Date Published:	1998-02-06
Start Page:	415
End Page:	423
Language:	English
DOI:	10.1016/s0092-8674(00)80933-2
PUBMED:	9476900
PROVIDER:	scopus
DOI/URL:	https://www.scopus.com/inward/record.uri?eid=2-s2.0-0032488847&doi=10.1016%2fS0092-8674%2800%2980933-2&partnerID=40&md5=ba4f45a623214176595a3647f135a22e
Notes:	Article -- Export Date: 12 December 2016 -- Source: Scopus

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