1azs
From Proteopedia
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|PDB= 1azs |SIZE=350|CAPTION= <scene name='initialview01'>1azs</scene>, resolution 2.3Å | |PDB= 1azs |SIZE=350|CAPTION= <scene name='initialview01'>1azs</scene>, resolution 2.3Å | ||
|SITE= <scene name='pdbsite=MGB:Mg+Binding+Site+In+Active+Site+Of+Adenylyl+Cyclase'>MGB</scene> | |SITE= <scene name='pdbsite=MGB:Mg+Binding+Site+In+Active+Site+Of+Adenylyl+Cyclase'>MGB</scene> | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=FKP:METHYLPIPERAZINOFORSKOLIN'>FKP</scene>, <scene name='pdbligand=GSP:5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
- | |ACTIVITY= [http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylate_cyclase Adenylate cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.6.1.1 4.6.1.1] </span> |
|GENE= ADENYLYL CYCLASE TYPE V ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris]), ADENYLYL CYCLASE TYPE II ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]), GNAS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | |GENE= ADENYLYL CYCLASE TYPE V ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 Canis lupus familiaris]), ADENYLYL CYCLASE TYPE II ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]), GNAS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1azs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1azs OCA], [http://www.ebi.ac.uk/pdbsum/1azs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1azs RCSB]</span> | ||
}} | }} | ||
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[[Category: Sprang, S R.]] | [[Category: Sprang, S R.]] | ||
[[Category: Tesmer, J J.G.]] | [[Category: Tesmer, J J.G.]] | ||
- | [[Category: FKP]] | ||
- | [[Category: GSP]] | ||
- | [[Category: MG]] | ||
[[Category: complex (lyase/hydrolase)]] | [[Category: complex (lyase/hydrolase)]] | ||
[[Category: cyclase]] | [[Category: cyclase]] | ||
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[[Category: signal transducing protein]] | [[Category: signal transducing protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:50:51 2008'' |
Revision as of 15:50, 30 March 2008
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, resolution 2.3Å | |||||||
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Sites: | |||||||
Ligands: | , , | ||||||
Gene: | ADENYLYL CYCLASE TYPE V (Canis lupus familiaris), ADENYLYL CYCLASE TYPE II (Rattus norvegicus), GNAS (Bos taurus) | ||||||
Activity: | Adenylate cyclase, with EC number 4.6.1.1 | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE
Overview
The crystal structure of a soluble, catalytically active form of adenylyl cyclase in a complex with its stimulatory heterotrimeric G protein alpha subunit (Gsalpha) and forskolin was determined to a resolution of 2.3 angstroms. When P-site inhibitors were soaked into native crystals of the complex, the active site of adenylyl cyclase was located and structural elements important for substrate recognition and catalysis were identified. On the basis of these and other structures, a molecular mechanism is proposed for the activation of adenylyl cyclase by Gsalpha.
About this Structure
1AZS is a Protein complex structure of sequences from Bos taurus, Canis lupus familiaris and Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS., Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR, Science. 1997 Dec 12;278(5345):1907-16. PMID:9417641
Page seeded by OCA on Sun Mar 30 18:50:51 2008