1nq3: Difference between revisions
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<StructureSection load='1nq3' size='340' side='right'caption='[[1nq3]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1nq3' size='340' side='right'caption='[[1nq3]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1nq3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1nq3]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Capra_hircus Capra hircus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NQ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NQ3 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">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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=1nq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nq3 OCA], [https://pdbe.org/1nq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nq3 RCSB], [https://www.ebi.ac.uk/pdbsum/1nq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nq3 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=1nq3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nq3 OCA], [https://pdbe.org/1nq3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nq3 RCSB], [https://www.ebi.ac.uk/pdbsum/1nq3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nq3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/RIDA_CAPHI RIDA_CAPHI] Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase.[UniProtKB:P52758] Also promotes endoribonucleolytic cleavage of some transcripts by promoting recruitment of the ribonuclease P/MRP complex. Acts by bridging YTHDF2 and the ribonuclease P/MRP complex. RIDA/HRSP12 binds to N6-methyladenosine (m6A)-containing mRNAs containing a 5'-GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such transcripts lead to recruitment of the ribonuclease P/MRP complex and subsequent endoribonucleolytic cleavage.[UniProtKB:P52758] | |||
== 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: Capra hircus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Briand | [[Category: Briand C]] | ||
[[Category: Deriu | [[Category: Deriu D]] | ||
[[Category: Grutter | [[Category: Grutter MG]] | ||
[[Category: Mistiniene | [[Category: Mistiniene E]] | ||
[[Category: Naktinis | [[Category: Naktinis V]] | ||
Latest revision as of 12:24, 16 August 2023
Crystal structure of the mammalian tumor associated antigen UK114Crystal structure of the mammalian tumor associated antigen UK114
Structural highlights
FunctionRIDA_CAPHI Catalyzes the hydrolytic deamination of enamine/imine intermediates that form during the course of normal metabolism. May facilitate the release of ammonia from these potentially toxic reactive metabolites, reducing their impact on cellular components. It may act on enamine/imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases including L-threonine dehydratase.[UniProtKB:P52758] Also promotes endoribonucleolytic cleavage of some transcripts by promoting recruitment of the ribonuclease P/MRP complex. Acts by bridging YTHDF2 and the ribonuclease P/MRP complex. RIDA/HRSP12 binds to N6-methyladenosine (m6A)-containing mRNAs containing a 5'-GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such transcripts lead to recruitment of the ribonuclease P/MRP complex and subsequent endoribonucleolytic cleavage.[UniProtKB:P52758] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe tumour-associated antigen UK114, isolated from goat liver, belongs to the YER057c/YIL051c/YjgF protein family, which has members in both the prokaryotes and eukaryotes. The crystal structure of a mammalian representative, goat UK114, was determined, revealing a trimeric arrangement in the crystal. It was confirmed by ultracentrifugation that UK114 is a trimer in solution. These results are in agreement with the published structures of homologues from unicellular organisms, but contrast with those reported for the rat homologue of UK114, for which a dimeric quaternary structure was proposed. Structure and oligomeric state of the mammalian tumour-associated antigen UK114.,Deriu D, Briand C, Mistiniene E, Naktinis V, Grutter MG Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1676-8. Epub 2003, Aug 19. PMID:12925811[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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