5bnf: Difference between revisions
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Apo structure of porcine CD38== | |||
<StructureSection load='5bnf' size='340' side='right'caption='[[5bnf]], [[Resolution|resolution]] 2.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5bnf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BNF FirstGlance]. <br> | |||
</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=5bnf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bnf OCA], [https://pdbe.org/5bnf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bnf RCSB], [https://www.ebi.ac.uk/pdbsum/5bnf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bnf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/F1S5D9_PIG F1S5D9_PIG] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cyclic ADP-ribose (cADPR) mobilizes intracellular Ca(2+) stores and activates Ca(2+) influx to regulate a wide range of physiological processes. It is one of the products produced from the catalysis of NAD(+) by the multifunctional CD38/ADP-ribosyl cyclase superfamily. After elimination of the nicotinamide ring by the enzyme, the reaction intermediate of NAD(+) can either be hydrolyzed to form linear ADPR or cyclized to form cADPR. We have previously shown that human CD38 exhibits a higher preference towards the hydrolysis of NAD(+) to form linear ADPR while Aplysia ADP-ribosyl cyclase prefers cyclizing NAD(+) to form cADPR. In this study, we characterized the enzymatic properties of porcine CD38 and revealed that it has a prominent secondary NAD(+) cyclase activity producing cADPR. We also determined the X-ray crystallographic structures of porcine CD38 and were able to observe conformational flexibility at the base of the active site of the enzyme which allow the NAD(+) reaction intermediate to adopt conformations resulting in both hydrolysis and cyclization forming linear ADPR and cADPR respectively. | |||
Porcine CD38 exhibits prominent secondary NAD(+) cyclase activity.,Ting KY, Leung CF, Graeff RM, Lee HC, Hao Q, Kotaka M Protein Sci. 2016 Mar;25(3):650-61. doi: 10.1002/pro.2859. Epub 2016 Jan 12. PMID:26660500<ref>PMID:26660500</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5bnf" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Kotaka | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Leung | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Sus scrofa]] | |||
[[Category: Graeff RM]] | |||
[[Category: Hao Q]] | |||
[[Category: Kotaka M]] | |||
[[Category: Lee HC]] | |||
[[Category: Leung CPF]] | |||
[[Category: Ting KY]] | |||
Latest revision as of 09:00, 7 June 2023
Apo structure of porcine CD38Apo structure of porcine CD38
Structural highlights
FunctionPublication Abstract from PubMedCyclic ADP-ribose (cADPR) mobilizes intracellular Ca(2+) stores and activates Ca(2+) influx to regulate a wide range of physiological processes. It is one of the products produced from the catalysis of NAD(+) by the multifunctional CD38/ADP-ribosyl cyclase superfamily. After elimination of the nicotinamide ring by the enzyme, the reaction intermediate of NAD(+) can either be hydrolyzed to form linear ADPR or cyclized to form cADPR. We have previously shown that human CD38 exhibits a higher preference towards the hydrolysis of NAD(+) to form linear ADPR while Aplysia ADP-ribosyl cyclase prefers cyclizing NAD(+) to form cADPR. In this study, we characterized the enzymatic properties of porcine CD38 and revealed that it has a prominent secondary NAD(+) cyclase activity producing cADPR. We also determined the X-ray crystallographic structures of porcine CD38 and were able to observe conformational flexibility at the base of the active site of the enzyme which allow the NAD(+) reaction intermediate to adopt conformations resulting in both hydrolysis and cyclization forming linear ADPR and cADPR respectively. Porcine CD38 exhibits prominent secondary NAD(+) cyclase activity.,Ting KY, Leung CF, Graeff RM, Lee HC, Hao Q, Kotaka M Protein Sci. 2016 Mar;25(3):650-61. doi: 10.1002/pro.2859. Epub 2016 Jan 12. PMID:26660500[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||