1r0s: Difference between revisions

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 ==Crystal structure of ADP-ribosyl cyclase Glu179Ala mutant==
-<StructureSection load='1r0s' size='340' side='right' caption='[[1r0s]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<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 [http://en.wikipedia.org/wiki/Aplca Aplca]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R0S FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1r12|1r12]], [[1r15|1r15]], [[1r16|1r16]], [[1lbe|1lbe]], [[1ism|1ism]], [[1isj|1isj]], [[1isi|1isi]], [[1ish|1ish]], [[1isg|1isg]]</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&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=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>
-<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=1r0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r0s OCA], [http://pdbe.org/1r0s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r0s RCSB], [http://www.ebi.ac.uk/pdbsum/1r0s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r0s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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]]
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 </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>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-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.
-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:15016363<ref>PMID:15016363</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1r0s" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Aplca]]
+[[Category: Aplysia californica]]
-[[Category: Graeff, R]]
+[[Category: Large Structures]]
-[[Category: Hao, Q]]
+[[Category: Graeff R]]
-[[Category: Kriksunov, I A]]
+[[Category: Hao Q]]
-[[Category: Lee, H C]]
+[[Category: Kriksunov IA]]
-[[Category: Love, M L]]
+[[Category: Lee HC]]
-[[Category: Munshi, C]]
+[[Category: Love ML]]
-[[Category: Szebenyi, D M.E]]
+[[Category: Munshi C]]
-[[Category: Thiel, D J]]
+[[Category: Szebenyi DME]]
-[[Category: Adp-ribosyl cyclase]]
+[[Category: Thiel DJ]]
-[[Category: Ca2+ signalling]]
-[[Category: Cyclic adp-ribose]]
-[[Category: Hydrolase]]
-[[Category: Naadp]]