View source for 4gr2


==Structure of AtRbcX1 from Arabidopsis thaliana.==
<StructureSection load='4gr2' size='340' side='right'caption='[[4gr2]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4gr2]] is a 2 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=4GR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GR2 FirstGlance]. <br>
</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=4gr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gr2 OCA], [https://pdbe.org/4gr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gr2 RCSB], [https://www.ebi.ac.uk/pdbsum/4gr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gr2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RBCX1_ARATH RBCX1_ARATH] Chaperone involved in RuBisCO assembly process.<ref>PMID:21922322</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Chloroplasts were formed by uptake of cyanobacteria into eukaryotic cells ca. 1.6billion years ago. During evolution most of the cyanobacterial genes were transferred from the chloroplast to the nuclear genome. The rbcX gene, encoding an assembly chaperone required for Rubisco biosynthesis in cyanobacteria, was duplicated. Here we demonstrate that homologous eukaryotic chaperones (AtRbcX1 and AtRbcX2) demonstrate different affinities for the C-terminus of Rubisco large subunit and determine their crystal structures. METHODS: Three-dimensional structures of AtRbcX1 and AtRbcX2 were resolved by the molecular replacement method. Equilibrium binding constants of the C-terminal RbcL peptide by AtRbcX proteins were determined by spectrofluorimetric titration. The binding mode of RbcX-RbcL was predicted using molecular dynamic simulation. RESULTS: We provide crystal structures of both chaperones from Arabidopsis thaliana providing the first structural insight into Rubisco assembly chaperones form higher plants. Despite the low sequence homology of eukaryotic and cyanobacterial Rubisco chaperones the eukaryotic counterparts exhibit surprisingly high similarity of the overall fold to previously determined prokaryotic structures. Modeling studies demonstrate that the overall mode of the binding of RbcL peptide is conserved among these proteins. As such, the evolution of RbcX chaperones is another example of maintaining conserved structural features despite significant drift in the primary amino acid sequence. GENERAL SIGNIFICANCE: The presented results are the approach to elucidate the role of RbcX proteins in Rubisco assembly in higher plants.

Insights into eukaryotic Rubisco assembly - Crystal structures of RbcX chaperones from Arabidopsis thaliana.,Kolesinski P, Golik P, Grudnik P, Piechota J, Markiewicz M, Tarnawski M, Dubin G, Szczepaniak A Biochim Biophys Acta. 2013 Jan 4. pii: S0304-4165(12)00386-8. doi:, 10.1016/j.bbagen.2012.12.025. PMID:23295968<ref>PMID:23295968</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4gr2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Dubin G]]
[[Category: Golik P]]
[[Category: Grudnik P]]
[[Category: Kolesinski P]]
[[Category: Szczepaniak A]]