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==COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MG==
==COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MG==
<StructureSection load='1cju' size='340' side='right' caption='[[1cju]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1cju' size='340' side='right'caption='[[1cju]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1cju]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin], [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Canlf Canlf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJU FirstGlance]. <br>
<table><tr><td colspan='2'>[[1cju]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DAD:2,3-DIDEOXYADENOSINE-5-TRIPHOSPHATE'>DAD</scene>, <scene name='pdbligand=FOK:FORSKOLIN'>FOK</scene>, <scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADENYLYL CYCLASE TYPE V ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9615 CANLF]), ADENYLYL CYCLASE TYPE II ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), GNAS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=DAD:2,3-DIDEOXYADENOSINE-5-TRIPHOSPHATE'>DAD</scene>, <scene name='pdbligand=FOK:FORSKOLIN'>FOK</scene>, <scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cju OCA], [https://pdbe.org/1cju PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cju RCSB], [https://www.ebi.ac.uk/pdbsum/1cju PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cju ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cju FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cju OCA], [http://pdbe.org/1cju PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cju RCSB], [http://www.ebi.ac.uk/pdbsum/1cju PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cju ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ADCY5_CANFA ADCY5_CANFA]] This is a membrane-bound, calcium-inhibitable adenylyl cyclase. [[http://www.uniprot.org/uniprot/GNAS2_BOVIN GNAS2_BOVIN]] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli. [[http://www.uniprot.org/uniprot/ADCY2_RAT ADCY2_RAT]] This is a membrane-bound, calmodulin-insensitive adenylyl cyclase.  
[https://www.uniprot.org/uniprot/ADCY5_CANLF ADCY5_CANLF] Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:1618857, PubMed:8428899, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion (By similarity).[UniProtKB:O95622]<ref>PMID:10427002</ref> <ref>PMID:11087399</ref> <ref>PMID:15591060</ref> <ref>PMID:1618857</ref> <ref>PMID:16766715</ref> <ref>PMID:19243146</ref> <ref>PMID:8428899</ref>  Lacks catalytic activity by itself, but can associate with isoform 1 to form active adenylyl cyclase.<ref>PMID:8428899</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 1cju" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1cju" style="background-color:#fffaf0;"></div>
==See Also==
*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Adenylate cyclase]]
[[Category: Bos taurus]]
[[Category: Bovin]]
[[Category: Canis lupus familiaris]]
[[Category: Buffalo rat]]
[[Category: Large Structures]]
[[Category: Canlf]]
[[Category: Rattus norvegicus]]
[[Category: Sprang, S R]]
[[Category: Sprang SR]]
[[Category: Tesmer, J J.G]]
[[Category: Tesmer JJG]]
[[Category: Cyclase]]
[[Category: Effector enzyme]]
[[Category: Hydrolase]]
[[Category: Lyase-lyase-signaling protein complex]]
[[Category: Signal transducing protein]]

Latest revision as of 14:04, 2 August 2023

COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MGCOMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP AND MG

Structural highlights

1cju is a 3 chain structure with sequence from Bos taurus, Canis lupus familiaris and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADCY5_CANLF Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling (PubMed:1618857, PubMed:8428899, PubMed:10427002, PubMed:11087399, PubMed:15591060, PubMed:16766715, PubMed:19243146). Mediates signaling downstream of ADRB1. Regulates the increase of free cytosolic Ca(2+) in response to increased blood glucose levels and contributes to the regulation of Ca(2+)-dependent insulin secretion (By similarity).[UniProtKB:O95622][1] [2] [3] [4] [5] [6] [7] Lacks catalytic activity by itself, but can associate with isoform 1 to form active adenylyl cyclase.[8]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Adenylyl cyclase (AC) converts adenosine triphosphate (ATP) to cyclic adenosine monophosphate, a ubiquitous second messenger that regulates many cellular functions. Recent structural studies have revealed much about the structure and function of mammalian AC but have not fully defined its active site or catalytic mechanism. Four crystal structures were determined of the catalytic domains of AC in complex with two different ATP analogs and various divalent metal ions. These structures provide a model for the enzyme-substrate complex and conclusively demonstrate that two metal ions bind in the active site. The similarity of the active site of AC to those of DNA polymerases suggests that the enzymes catalyze phosphoryl transfer by the same two-metal-ion mechanism and likely have evolved from a common ancestor.

Two-metal-Ion catalysis in adenylyl cyclase.,Tesmer JJ, Sunahara RK, Johnson RA, Gosselin G, Gilman AG, Sprang SR Science. 1999 Jul 30;285(5428):756-60. PMID:10427002[9]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Tesmer JJ, Sunahara RK, Johnson RA, Gosselin G, Gilman AG, Sprang SR. Two-metal-Ion catalysis in adenylyl cyclase. Science. 1999 Jul 30;285(5428):756-60. PMID:10427002
  2. ↑ Tesmer JJ, Dessauer CW, Sunahara RK, Murray LD, Johnson RA, Gilman AG, Sprang SR. Molecular basis for P-site inhibition of adenylyl cyclase. Biochemistry. 2000 Nov 28;39(47):14464-71. PMID:11087399
  3. ↑ Mou TC, Gille A, Fancy DA, Seifert R, Sprang SR. Structural basis for the inhibition of mammalian membrane adenylyl cyclase by 2 '(3')-O-(N-Methylanthraniloyl)-guanosine 5 '-triphosphate. J Biol Chem. 2005 Feb 25;280(8):7253-61. Epub 2004 Dec 9. PMID:15591060 doi:http://dx.doi.org/10.1074/jbc.M409076200
  4. ↑ Ishikawa Y, Katsushika S, Chen L, Halnon NJ, Kawabe J, Homcy CJ. Isolation and characterization of a novel cardiac adenylylcyclase cDNA. J Biol Chem. 1992 Jul 5;267(19):13553-7. PMID:1618857
  5. ↑ Mou TC, Gille A, Suryanarayana S, Richter M, Seifert R, Sprang SR. Broad specificity of mammalian adenylyl cyclase for interaction with 2',3'-substituted purine- and pyrimidine nucleotide inhibitors. Mol Pharmacol. 2006 Sep;70(3):878-86. Epub 2006 Jun 9. PMID:16766715 doi:http://dx.doi.org/10.1124/mol.106.026427
  6. ↑ Mou TC, Masada N, Cooper DM, Sprang SR. Structural basis for inhibition of mammalian adenylyl cyclase by calcium. Biochemistry. 2009 Apr 21;48(15):3387-97. PMID:19243146 doi:http://dx.doi.org/10.1021/bi802122k
  7. ↑ Katsushika S, Kawabe J, Homcy CJ, Ishikawa Y. In vivo generation of an adenylylcyclase isoform with a half-molecule motif. J Biol Chem. 1993 Feb 5;268(4):2273-6. PMID:8428899
  8. ↑ Katsushika S, Kawabe J, Homcy CJ, Ishikawa Y. In vivo generation of an adenylylcyclase isoform with a half-molecule motif. J Biol Chem. 1993 Feb 5;268(4):2273-6. PMID:8428899
  9. ↑ Tesmer JJ, Sunahara RK, Johnson RA, Gosselin G, Gilman AG, Sprang SR. Two-metal-Ion catalysis in adenylyl cyclase. Science. 1999 Jul 30;285(5428):756-60. PMID:10427002

1cju, resolution 2.80Å

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