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3maa

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Revision as of 07:38, 25 December 2014

Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5-O-(l-Thiophosphate) and Low Ca Concentration

Structural highlights

3maa is a 3 chain structure with sequence from Bos taurus, Canis lupus familiaris and Rattus norvegicus. This structure supersedes the now removed PDB entry 3e8a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Related:	3c16, 3c15, 3c14
Gene:	ADCY5, ADENYLYL CYCLASE TYPE V (Canis lupus familiaris), Adcy2, ADENYLYL CYCLASE TYPE II (Rattus norvegicus), GNAS, GNAS1 (Bos taurus)
Activity:	Adenylate cyclase, with EC number 4.6.1.1
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[ADCY5_CANFA] This is a membrane-bound, calcium-inhibitable adenylyl cyclase. [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. [ADCY2_RAT] This is a membrane-bound, calmodulin-insensitive adenylyl cyclase.

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

Type V and VI mammalian adenylyl cyclases (AC5, AC6) are inhibited by Ca(2+) at both sub- and supramicromolar concentration. This inhibition may provide feedback in situations where cAMP promotes opening of Ca(2+) channels, allowing fine control of cardiac contraction and rhythmicity in cardiac tissue where AC5 and AC6 predominate. Ca(2+) inhibits the soluble AC core composed of the C1 domain of AC5 (VC1) and the C2 domain of AC2 (IIC2). As observed for holo-AC5, inhibition is biphasic, showing "high-affinity" (K(i) = approximately 0.4 microM) and "low-affinity" (K(i) = approximately 100 microM) modes of inhibition. At micromolar concentration, Ca(2+) inhibition is nonexclusive with respect to pyrophosphate (PP(i)), a noncompetitive inhibitor with respect to ATP, but at >100 microM Ca(2+), inhibition appears to be exclusive with respect to PP(i). The 3.0 A resolution structure of Galphas.GTPgammaS/forskolin-activated VC1:IIC2 crystals soaked in the presence of ATPalphaS and 8 microM free Ca(2+) contains a single, loosely coordinated metal ion. ATP soaked into VC1:IIC2 crystals in the presence of 1.5 mM Ca(2+) is not cyclized, and two calcium ions are observed in the 2.9 A resolution structure of the complex. In both of the latter complexes VC1:IIC2 adopts the "open", catalytically inactive conformation characteristic of the apoenzyme, in contrast to the "closed", active conformation seen in the presence of ATP analogues and Mg(2+) or Mn(2+). Structures of the pyrophosphate (PP(i)) complex with 10 mM Mg(2+) (2.8 A) or 2 mM Ca(2+) (2.7 A) also adopt the open conformation, indicating that the closed to open transition occurs after cAMP release. In the latter complexes, Ca(2+) and Mg(2+) bind only to the high-affinity "B" metal site associated with substrate/product stabilization. Ca(2+) thus stabilizes the inactive conformation in both ATP- and PP(i)-bound states.

Structural basis for inhibition of mammalian adenylyl cyclase by calcium.,Mou TC, Masada N, Cooper DM, Sprang SR Biochemistry. 2009 Apr 21;48(15):3387-97. PMID:19243146^[1]

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

References

↑ 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

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/3maa"

@@ Line 9: / Line 9: @@
 <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=3maa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3maa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3maa RCSB], [http://www.ebi.ac.uk/pdbsum/3maa PDBsum]</span></td></tr>
 </table>
+== 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3maa

From Proteopedia

Revision as of 07:38, 25 December 2014

Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5-O-(l-Thiophosphate) and Low Ca Concentration

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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