1r0s: Difference between revisions

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New page: left|200px<br /><applet load="1r0s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r0s, resolution 2.0Å" /> '''Crystal structure of ...
 
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[[Image:1r0s.jpg|left|200px]]<br /><applet load="1r0s" size="450" color="white" frame="true" align="right" spinBox="true"
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'''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://ispc.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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:10:25 2007''

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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