1re0
From Proteopedia
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- | [[Image:1re0.jpg|left|200px]] | + | [[Image:1re0.jpg|left|200px]] |
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- | '''Structure of ARF1-GDP bound to Sec7 domain complexed with Brefeldin A''' | + | {{Structure |
+ | |PDB= 1re0 |SIZE=350|CAPTION= <scene name='initialview01'>1re0</scene>, resolution 2.40Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=AFB:1,6,7,8,9,11A,12,13,14,14A-DECAHYDRO-1,13-DIHYDROXY-6-METHYL-4H-CYCLOPENT[F]OXACYCLOTRIDECIN-4-ONE'>AFB</scene> and <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= ARF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), Gea1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
+ | }} | ||
+ | |||
+ | '''Structure of ARF1-GDP bound to Sec7 domain complexed with Brefeldin A''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1RE0 is a [ | + | 1RE0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RE0 OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism., Mossessova E, Corpina RA, Goldberg J, Mol Cell. 2003 Dec;12(6):1403-11. PMID:[http:// | + | Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism., Mossessova E, Corpina RA, Goldberg J, Mol Cell. 2003 Dec;12(6):1403-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14690595 14690595] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: alph-beta]] | [[Category: alph-beta]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:50:22 2008'' |
Revision as of 11:50, 20 March 2008
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, resolution 2.40Å | |||||||
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Ligands: | , , and | ||||||
Gene: | ARF1 (Homo sapiens), Gea1 (Saccharomyces cerevisiae) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Structure of ARF1-GDP bound to Sec7 domain complexed with Brefeldin A
Overview
ARF GTPases are activated by guanine nucleotide exchange factors (GEFs) of the Sec7 family that promote the exchange of GDP for GTP. Brefeldin A (BFA) is a fungal metabolite that binds to the ARF1*GDP*Sec7 complex and blocks GEF activity at an early stage of the reaction, prior to guanine nucleotide release. The crystal structure of the ARF1*GDP*Sec7*BFA complex shows that BFA binds at the protein-protein interface to inhibit conformational changes in ARF1 required for Sec7 to dislodge the GDP molecule. Based on a comparative analysis of the inhibited complex, nucleotide-free ARF1*Sec7 and ARF1*GDP, we suggest that, in addition to forcing nucleotide release, the ARF1-Sec7 binding energy is used to open a cavity on ARF1 to facilitate the rearrangement of hydrophobic core residues between the GDP and GTP conformations. Thus, the Sec7 domain may act as a dual catalyst, facilitating both nucleotide release and conformational switching on ARF proteins.
About this Structure
1RE0 is a Protein complex structure of sequences from Homo sapiens and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of ARF1*Sec7 complexed with Brefeldin A and its implications for the guanine nucleotide exchange mechanism., Mossessova E, Corpina RA, Goldberg J, Mol Cell. 2003 Dec;12(6):1403-11. PMID:14690595
Page seeded by OCA on Thu Mar 20 13:50:22 2008
Categories: Homo sapiens | Protein complex | Saccharomyces cerevisiae | Goldberg, J. | Mossessova, E. | AFB | CIT | GDP | MG | All-helical | Alph-beta