1cjv

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Current revision

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

Structural highlights

1cjv 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 3Å
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.

References

↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cjv"

@@ Line 1: / Line 1: @@
-[[Image:1cjv.gif|left|200px]]<br /><applet load="1cjv" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1cjv, resolution 3.00&Aring;" />
-'''COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP, MG, AND ZN'''<br />
-==Overview==
+==COMPLEX OF GS-ALPHA WITH THE CATALYTIC DOMAINS OF MAMMALIAN ADENYLYL CYCLASE: COMPLEX WITH BETA-L-2',3'-DIDEOXYATP, MG, AND ZN==
-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.
+<StructureSection load='1cjv' size='340' side='right'caption='[[1cjv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1cjv]] 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=1CJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CJV FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1cjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cjv OCA], [https://pdbe.org/1cjv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cjv RCSB], [https://www.ebi.ac.uk/pdbsum/1cjv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cjv ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/1cjv_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cjv ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==About this Structure==
+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<ref>PMID:10427002</ref>
-CJV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus], [http://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris] and [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG, CL, ZN, GSP, FOK, DAD and MES as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CJV OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10427002 10427002]
+</div>
-[[Category: Adenylate cyclase]]
+<div class="pdbe-citations 1cjv" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[3D Adenylyl cyclase 3D structures|3D Adenylyl cyclase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Bos taurus]]
 [[Category: Canis lupus familiaris]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
 [[Category: Rattus norvegicus]]
-[[Category: Sprang, S.R.]]
+[[Category: Sprang SR]]
-[[Category: Tesmer, J.J.G.]]
+[[Category: Tesmer JJG]]
-[[Category: CL]]
-[[Category: DAD]]
-[[Category: FOK]]
-[[Category: GSP]]
-[[Category: MES]]
-[[Category: MG]]
-[[Category: ZN]]
-[[Category: complex (lyase/hydrolase)]]
-[[Category: cyclase]]
-[[Category: effector enzyme]]
-[[Category: hydrolase]]
-[[Category: signal transducing protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:31:24 2007''

1cjv

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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