3rg6: Difference between revisions
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==Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco== | ==Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco== | ||
<StructureSection load='3rg6' size='340' side='right' caption='[[3rg6]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='3rg6' size='340' side='right'caption='[[3rg6]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3rg6]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3rg6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] and [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_6301 Synechococcus elongatus PCC 6301]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RG6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RG6 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]] 3.2Å</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=3rg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rg6 OCA], [https://pdbe.org/3rg6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rg6 RCSB], [https://www.ebi.ac.uk/pdbsum/3rg6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rg6 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/RBL_SYNP6 RBL_SYNP6] RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3rg6" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[RuBisCO|RuBisCO]] | *[[RuBisCO 3D structures|RuBisCO 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Anabaena sp]] | [[Category: Anabaena sp]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synechococcus elongatus PCC 6301]] | ||
[[Category: Bracher | [[Category: Bracher A]] | ||
[[Category: Hartl | [[Category: Hartl FU]] | ||
[[Category: Hayer-Hartl | [[Category: Hayer-Hartl M]] | ||
[[Category: Starling-Windhof | [[Category: Starling-Windhof A]] | ||
Latest revision as of 05:21, 21 November 2024
Crystal structure of a chaperone-bound assembly intermediate of form I RubiscoCrystal structure of a chaperone-bound assembly intermediate of form I Rubisco
Structural highlights
FunctionRBL_SYNP6 RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338] Publication Abstract from PubMedThe form I Rubisco of autotrophic bacteria, algae and plants is a complex of eight large (RbcL) and eight small (RbcS) subunits. It fixes atmospheric CO(2) in the dark reaction of photosynthesis. As shown for the cyanobacterial enzyme, folding of the RbcL subunits is mediated by the GroEL-GroES chaperonin system, and assembly requires the specialized chaperone RbcX, a homodimer of ~15-kDa subunits. Here we present the 3.2-A crystal structure of a Rubisco assembly intermediate, consisting of the RbcL(8) core with eight RbcX(2) molecules bound. The structure reveals the molecular mechanism by which RbcX(2) mediates oligomeric assembly. Specifically, RbcX(2) provides positional information for proper formation of antiparallel RbcL dimers, thereby preventing RbcL-RbcL misalignment and off-pathway aggregation. The RbcL(8)(RbcX(2))(8) structure also suggests that RbcS functions by stabilizing the '60s loop' of RbcL in the catalytically active conformation. Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco.,Bracher A, Starling-Windhof A, Hartl FU, Hayer-Hartl M Nat Struct Mol Biol. 2011 Jul 17. doi: 10.1038/nsmb.2090. PMID:21765418[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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