View source for 6uew


==Rubisco / CsoS2 N-peptide complex responsible for alpha-carboxysome cargo loading==
<StructureSection load='6uew' size='340' side='right'caption='[[6uew]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6uew]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Halothiobacillus_neapolitanus_c2 Halothiobacillus neapolitanus c2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UEW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UEW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</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=6uew FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uew OCA], [https://pdbe.org/6uew PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uew RCSB], [https://www.ebi.ac.uk/pdbsum/6uew PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uew ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBL1_HALNC RBL1_HALNC] 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. Both reactions occur simultaneously and in competition at the same active site.[HAMAP-Rule:MF_01338]
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== Publication Abstract from PubMed ==
Carboxysomes are bacterial microcompartments that function as the centerpiece of the bacterial CO2-concentrating mechanism by facilitating high CO2 concentrations near the carboxylase Rubisco. The carboxysome self-assembles from thousands of individual proteins into icosahedral-like particles with a dense enzyme cargo encapsulated within a proteinaceous shell. In the case of the alpha-carboxysome, there is little molecular insight into protein-protein interactions that drive the assembly process. Here, studies on the alpha-carboxysome from Halothiobacillus neapolitanus demonstrate that Rubisco interacts with the N terminus of CsoS2, a multivalent, intrinsically disordered protein. X-ray structural analysis of the CsoS2 interaction motif bound to Rubisco reveals a series of conserved electrostatic interactions that are only made with properly assembled hexadecameric Rubisco. Although biophysical measurements indicate that this single interaction is weak, its implicit multivalency induces high-affinity binding through avidity. Taken together, our results indicate that CsoS2 acts as an interaction hub to condense Rubisco and enable efficient alpha-carboxysome formation.

Multivalent interactions between CsoS2 and Rubisco mediate alpha-carboxysome formation.,Oltrogge LM, Chaijarasphong T, Chen AW, Bolin ER, Marqusee S, Savage DF Nat Struct Mol Biol. 2020 Mar;27(3):281-287. doi: 10.1038/s41594-020-0387-7. Epub, 2020 Mar 2. PMID:32123388<ref>PMID:32123388</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6uew" style="background-color:#fffaf0;"></div>

==See Also==
*[[RuBisCO 3D structures|RuBisCO 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Halothiobacillus neapolitanus c2]]
[[Category: Large Structures]]
[[Category: Oltrogge LM]]
[[Category: Savage DF]]