2i3e: Difference between revisions
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==Solution structure of catalytic domain of goldfish RICH protein== | ==Solution structure of catalytic domain of goldfish RICH protein== | ||
<StructureSection load='2i3e' size='340' side='right'caption='[[2i3e | <StructureSection load='2i3e' size='340' side='right'caption='[[2i3e]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2i3e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2i3e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carassius_auratus Carassius auratus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I3E FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2i3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3e OCA], [https://pdbe.org/2i3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i3e RCSB], [https://www.ebi.ac.uk/pdbsum/2i3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i3e ProSAT]</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=2i3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i3e OCA], [https://pdbe.org/2i3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i3e RCSB], [https://www.ebi.ac.uk/pdbsum/2i3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i3e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q90306_CARAU Q90306_CARAU] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Carassius auratus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Denisov | [[Category: Denisov AY]] | ||
[[Category: Gehring | [[Category: Gehring K]] | ||
[[Category: Kozlov | [[Category: Kozlov G]] | ||
Latest revision as of 22:03, 29 May 2024
Solution structure of catalytic domain of goldfish RICH proteinSolution structure of catalytic domain of goldfish RICH protein
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedRegeneration-induced CNPase homolog (RICH) is an axonal growth-associated protein, which is induced in teleost fish upon optical nerve injury. RICH consists of a highly acidic N-terminal domain, a catalytic domain with 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) activity and a C-terminal isoprenylation site. In vitro RICH and mammalian brain CNPase specifically catalyze the hydrolysis of 2',3'-cyclic nucleotides to produce 2'-nucleotides, but the physiologically relevant in vivo substrate remains unknown. Here, we report the NMR structure of the catalytic domain of goldfish RICH and describe its binding to CNPase inhibitors. The structure consists of a twisted nine-stranded antiparallel beta-sheet surrounded by alpha-helices on both sides. Despite significant local differences mostly arising from a seven-residue insert in the RICH sequence, the active site region is highly similar to that of human CNPase. Likewise, refinement of the catalytic domain of rat CNPase using residual dipolar couplings gave improved agreement with the published crystal structure. NMR titrations of RICH with inhibitors point to a similar catalytic mechanism for RICH and CNPase. The results suggest a functional importance for the evolutionarily conserved phosphodiesterase activity and hint of a link with pre-tRNA splicing. Solution structure of the catalytic domain of RICH protein from goldfish.,Kozlov G, Denisov AY, Pomerantseva E, Gravel M, Braun PE, Gehring K FEBS J. 2007 Mar;274(6):1600-9. PMID:17480208[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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