4wt3: Difference between revisions
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==The N-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana== | ==The N-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana== | ||
<StructureSection load='4wt3' size='340' side='right' caption='[[4wt3]], [[Resolution|resolution]] 1.95Å' scene=''> | <StructureSection load='4wt3' size='340' side='right'caption='[[4wt3]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wt3]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4wt3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WT3 FirstGlance]. <br> | ||
</td></tr> | </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=4wt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wt3 OCA], [https://pdbe.org/4wt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wt3 RCSB], [https://www.ebi.ac.uk/pdbsum/4wt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wt3 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/RAF2_ARATH RAF2_ARATH] Required for assembly or stability of RuBisCO. Acts at a postchaperonin step to fold and/or assemble the large subunit (LS) into RuBisCO (By similarity). | ||
<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: Arabidopsis thaliana]] | ||
[[Category: Bhat | [[Category: Large Structures]] | ||
[[Category: Bracher | [[Category: Bhat JY]] | ||
[[Category: Hartl | [[Category: Bracher A]] | ||
[[Category: Hauser | [[Category: Hartl FU]] | ||
[[Category: Hayer-Hartl | [[Category: Hauser T]] | ||
[[Category: Milicic | [[Category: Hayer-Hartl M]] | ||
[[Category: Wendler | [[Category: Milicic G]] | ||
[[Category: Wendler P]] | |||
Revision as of 10:24, 7 April 2023
The N-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thalianaThe N-terminal domain of Rubisco Accumulation Factor 1 from Arabidopsis thaliana
Structural highlights
FunctionRAF2_ARATH Required for assembly or stability of RuBisCO. Acts at a postchaperonin step to fold and/or assemble the large subunit (LS) into RuBisCO (By similarity). Publication Abstract from PubMedBiogenesis of the photosynthetic enzyme Rubisco, a complex of eight large (RbcL) and eight small (RbcS) subunits, requires assembly chaperones. Here we analyzed the role of Rubisco accumulation factor1 (Raf1), a dimer of approximately 40-kDa subunits. We find that Raf1 from Synechococcus elongatus acts downstream of chaperonin-assisted RbcL folding by stabilizing RbcL antiparallel dimers for assembly into RbcL8 complexes with four Raf1 dimers bound. Raf1 displacement by RbcS results in holoenzyme formation. Crystal structures show that Raf1 from Arabidopsis thaliana consists of a beta-sheet dimerization domain and a flexibly linked alpha-helical domain. Chemical cross-linking and EM reconstruction indicate that the beta-domains bind along the equator of each RbcL2 unit, and the alpha-helical domains embrace the top and bottom edges of RbcL2. Raf1 fulfills a role similar to that of the assembly chaperone RbcX, thus suggesting that functionally redundant factors ensure efficient Rubisco biogenesis. Structure and mechanism of the Rubisco-assembly chaperone Raf1.,Hauser T, Bhat JY, Milicic G, Wendler P, Hartl FU, Bracher A, Hayer-Hartl M Nat Struct Mol Biol. 2015 Aug 3. doi: 10.1038/nsmb.3062. PMID:26237510[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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