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[[Image:1r0s.jpg|left|200px]]<br /><applet load="1r0s" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1r0s, resolution 2.0&Aring;" />
'''Crystal structure of ADP-ribosyl cyclase Glu179Ala mutant'''<br />


==Overview==
==Crystal structure of ADP-ribosyl cyclase Glu179Ala mutant==
ADP-ribosyl cyclase catalyzes the elimination of nicotinamide from NAD and cyclization to cADPR, a known second messenger in cellular calcium signaling pathways. We have determined to 2.0 A resolution the structure of Aplysia cyclase with ribose-5-phosphate bound covalently at C3' and with the base exchange substrate (BES), pyridylcarbinol, bound to the active site. In addition, further refinement at 2.4 A resolution of the structure of nicotinamide-bound cyclase, which was previously reported, reveals that ribose-5-phosphate is also covalently bound in this structure, and a second nicotinamide site was identified. The structures of native and mutant Glu179Ala cyclase were also solved to 1.7 and 2.0 A respectively. It is proposed that the second nicotinamide site serves to promote cyclization by clearing the active site of the nicotinamide byproduct. Moreover, a ribosylation mechanism can be proposed in which the cyclization reaction proceeds through a covalently bound intermediate.
<StructureSection load='1r0s' size='340' side='right'caption='[[1r0s]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1r0s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R0S 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]] 2&#8491;</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=1r0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0s OCA], [https://pdbe.org/1r0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r0s RCSB], [https://www.ebi.ac.uk/pdbsum/1r0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r0s ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/NADA_APLCA NADA_APLCA] Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for calcium mobilization from endoplasmic reticulum. Also has cADPr hydrolase activity.<ref>PMID:11829748</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/r0/1r0s_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=1r0s ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1R0S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_californica Aplysia californica]. Active as [http://en.wikipedia.org/wiki/NAD(+)_nucleosidase NAD(+) nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.5 3.2.2.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R0S OCA].
*[[Cluster of Differentiation CD38|Cluster of Differentiation CD38]]
 
== References ==
==Reference==
<references/>
ADP-ribosyl cyclase; crystal structures reveal a covalent intermediate., Love ML, Szebenyi DM, Kriksunov IA, Thiel DJ, Munshi C, Graeff R, Lee HC, Hao Q, Structure. 2004 Mar;12(3):477-86. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15016363 15016363]
__TOC__
</StructureSection>
[[Category: Aplysia californica]]
[[Category: Aplysia californica]]
[[Category: NAD(+) nucleosidase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Graeff R]]
[[Category: Graeff, R.]]
[[Category: Hao Q]]
[[Category: Hao, Q.]]
[[Category: Kriksunov IA]]
[[Category: Kriksunov, I A.]]
[[Category: Lee HC]]
[[Category: Lee, H C.]]
[[Category: Love ML]]
[[Category: Love, M L.]]
[[Category: Munshi C]]
[[Category: Munshi, C.]]
[[Category: Szebenyi DME]]
[[Category: Szebenyi, D M.E.]]
[[Category: Thiel DJ]]
[[Category: Thiel, D J.]]
[[Category: adp-ribosyl cyclase]]
[[Category: ca2+ signalling]]
[[Category: cyclic adp-ribose]]
[[Category: naadp]]
[[Category: x-ray crystallography]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:45 2008''

Latest revision as of 09:08, 17 April 2024

Crystal structure of ADP-ribosyl cyclase Glu179Ala mutantCrystal structure of ADP-ribosyl cyclase Glu179Ala mutant

Structural highlights

1r0s is a 2 chain structure with sequence from Aplysia californica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NADA_APLCA Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger for calcium mobilization from endoplasmic reticulum. Also has cADPr hydrolase activity.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Chini EN, Chini CC, Kato I, Takasawa S, Okamoto H. CD38 is the major enzyme responsible for synthesis of nicotinic acid-adenine dinucleotide phosphate in mammalian tissues. Biochem J. 2002 Feb 15;362(Pt 1):125-30. PMID:11829748

1r0s, resolution 2.00Å

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