PMID- 10102276
OWN - NLM
STAT- MEDLINE
DCOM- 19990427
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 96
IP  - 6
DP  - 1999 Mar 19
TI  - Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for 
      coatomer in GTP hydrolysis.
PG  - 893-902
AB  - The crystal structure of the complex of ARF1 GTPase bound to GDP and the
      catalytic domain of ARF GTPase-activating protein (ARFGAP) has been determined at
      1.95 A resolution. The ARFGAP molecule binds to switch 2 and helix alpha3 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.
FAU - Goldberg, J
AU  - Goldberg J
AD  - Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer
      Center, New York, New York 10021, USA. jonathan@ximpact4.ski.mskcc.org
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Coatomer Protein)
RN  - 0 (GTPase-Activating Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Proteins)
RN  - 0 (ras GTPase-Activating Proteins)
RN  - 86-01-1 (Guanosine Triphosphate)
RN  - 94ZLA3W45F (Arginine)
RN  - EC 3.6.1.- (GTP Phosphohydrolases)
RN  - EC 3.6.1.- (GTP-Binding Proteins)
RN  - EC 3.6.5.2 (ADP-Ribosylation Factor 1)
RN  - EC 3.6.5.2 (ADP-Ribosylation Factors)
RN  - EC 3.6.5.2 (ras Proteins)
SB  - IM
MH  - ADP-Ribosylation Factor 1
MH  - ADP-Ribosylation Factors
MH  - Amino Acid Sequence
MH  - Animals
MH  - Arginine
MH  - Coatomer Protein
MH  - GTP Phosphohydrolases/*metabolism
MH  - GTP-Binding Proteins/chemistry/metabolism/*physiology
MH  - GTPase-Activating Proteins
MH  - Guanosine Triphosphate/*metabolism
MH  - Humans
MH  - Hydrolysis
MH  - Membrane Proteins/*metabolism
MH  - Molecular Sequence Data
MH  - Protein Conformation
MH  - Proteins/chemistry/metabolism/*physiology
MH  - Rats
MH  - Sequence Homology, Amino Acid
MH  - Structure-Activity Relationship
MH  - ras GTPase-Activating Proteins
MH  - ras Proteins/chemistry/*metabolism
EDAT- 1999/04/02 00:00
MHDA- 1999/04/02 00:01
CRDT- 1999/04/02 00:00
PHST- 1999/04/02 00:00 [pubmed]
PHST- 1999/04/02 00:01 [medline]
PHST- 1999/04/02 00:00 [entrez]
AID - S0092-8674(00)80598-X [pii]
AID - 10.1016/s0092-8674(00)80598-x [doi]
PST - ppublish
SO  - Cell. 1999 Mar 19;96(6):893-902. doi: 10.1016/s0092-8674(00)80598-x.