3k80: Difference between revisions
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<StructureSection load='3k80' size='340' side='right'caption='[[3k80]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3k80' size='340' side='right'caption='[[3k80]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3k80]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3k80]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lama_glama Lama glama] and [https://en.wikipedia.org/wiki/Trypanosoma_brucei Trypanosoma brucei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K80 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K80 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]] 2.4Å</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=3k80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k80 OCA], [https://pdbe.org/3k80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k80 RCSB], [https://www.ebi.ac.uk/pdbsum/3k80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k80 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=3k80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k80 OCA], [https://pdbe.org/3k80 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k80 RCSB], [https://www.ebi.ac.uk/pdbsum/3k80 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k80 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q38B90_TRYB2 Q38B90_TRYB2] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Lama glama]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Trypanosoma brucei]] | ||
[[Category: | [[Category: Wu M]] | ||
Latest revision as of 11:11, 6 September 2023
Structure of essential protein from Trypanosoma bruceiStructure of essential protein from Trypanosoma brucei
Structural highlights
FunctionPublication Abstract from PubMedSeveral major global diseases are caused by single-cell parasites called trypanosomatids. These organisms exhibit many unusual features including a unique and essential U-insertion/deletion RNA editing process in their single mitochondrion. Many key RNA editing steps occur in approximately 20S editosomes, which have a core of 12 proteins. Among these, the "interaction protein" KREPA6 performs a central role in maintaining the integrity of the editosome core and also binds to ssRNA. The use of llama single domain antibodies (VHH domains) accelerated crystal growth of KREPA6 from Trypanosoma brucei dramatically. All three structures obtained are heterotetramers with a KREPA6 dimer in the center, and one VHH domain bound to each KREPA6 subunit. Two of the resultant heterotetramers use complementarity determining region 2 (CDR2) and framework residues to form a parallel pair of beta strands with KREPA6 - a mode of interaction not seen before in VHH domain-protein antigen complexes. The third type of VHH domain binds in a totally different manner to KREPA6. Intriguingly, while KREPA6 forms tetramers in solution adding either one of the three VHH domains results in the formation of a heterotetramer in solution, in perfect agreement with the crystal structures. Biochemical solution studies indicate that the C-terminal tail of KREPA6 is involved in the dimerization of KREPA6 dimers to form tetramers. The implications of these crystallographic and solution studies for possible modes of interaction of KREPA6 with its many binding partners in the editosome are discussed. Structures of a key interaction protein from the Trypanosoma brucei editosome in complex with single domain antibodies.,Wu M, Park YJ, Pardon E, Turley S, Hayhurst A, Deng J, Steyaert J, Hol WG J Struct Biol. 2010 Oct 20. PMID:20969962[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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