Structural and functional analysis of the ARF1-aRFGAP complex reveals a role for coatomer in GTP hydrolysis Journal Article
| Author: | Goldberg, J. |
| Article Title: | Structural and functional analysis of the ARF1-aRFGAP complex reveals a role for coatomer in GTP hydrolysis |
| Abstract: | The crystal structure of the complex of ARFI GTPase bound to GDP and the catalytic domain of ARF GTPase-activating protein (ARFGAP) has been determined at 1.95 Å resolution. The ARFGAP molecule binds to switch 2 and helix α3 to orient ARF1 residues for catalysis, but it supplies neither arginine nor other amino acid side chains to the GTPase active site. In the complex, the effector-binding region appears to be unobstructed, suggesting that ARFGAP could stimulate GTP hydrolysis while ARF1 maintains an interaction with its effector, the coatomer complex of COPI-coated vesicles. Biochemical experiments show that coatomer directly participates in the GTPase reaction, accelerating GTP hydrolysis a further 1000-fold in an ARFGAP-dependent manner. Thus, a tripartite complex controls the GTP hydrolysis reaction triggering disassembly of COPI vesicle coats. |
| Keywords: | nonhuman; protein conformation; proteins; animals; cell protein; gtp-binding proteins; membrane proteins; structure-activity relationship; amino acid sequence; molecular sequence data; sequence homology, amino acid; gtpase-activating proteins; crystal structure; rats; ras proteins; catalysis; enzyme binding; enzyme structure; guanosine triphosphate; hydrolysis; arginine; gtp phosphohydrolases; enzyme active site; guanosine diphosphate; guanosine triphosphatase; coatomer protein; coat protein; adp-ribosylation factor 1; adp-ribosylation factors; humans; human; priority journal; article; ras gtpase-activating proteins |
| Journal Title: | Cell |
| Volume: | 96 |
| Issue: | 6 |
| ISSN: | 0092-8674 |
| Publisher: | Cell Press |
| Date Published: | 1999-03-19 |
| Start Page: | 893 |
| End Page: | 902 |
| Language: | English |
| PUBMED: | 10102276 |
| PROVIDER: | scopus |
| DOI: | 10.1016/S0092-8674(00)80598-X |
| DOI/URL: | |
| Notes: | Article -- Export Date: 16 August 2016 -- Source: Scopus |
