View source for 6zxt


==High resolution crystal structure of chloroplastic ribose-5-phosphate isomerase from Chlamydomonas reinhardtii==
<StructureSection load='6zxt' size='340' side='right'caption='[[6zxt]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6zxt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZXT 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]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6zxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zxt OCA], [https://pdbe.org/6zxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zxt RCSB], [https://www.ebi.ac.uk/pdbsum/6zxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zxt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8IRQ1_CHLRE A8IRQ1_CHLRE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Calvin-Benson cycle is the key metabolic pathway of photosynthesis responsible for carbon fixation and relies on eleven conserved enzymes. Ribose-5-phosphate isomerase (RPI) isomerizes ribose-5-phosphate into ribulose-5-phosphate and contributes to the regeneration of the Rubisco substrate. Plant RPI is the target of diverse post-translational modifications including phosphorylation and thiol-based modifications to presumably adjust its activity to the photosynthetic electron flow. Here, we describe the first experimental structure of a photosynthetic RPI at 1.4 A resolution. Our structure confirms the composition of the catalytic pocket of the enzyme. We describe the homo-dimeric state of the protein that we observed in the crystal and in solution. We also map the positions of previously reported post-translational modifications and propose mechanisms by which they may impact the catalytic parameters. The structural data will inform the biochemical modeling of photosynthesis.

High-Resolution Crystal Structure of Chloroplastic Ribose-5-Phosphate Isomerase from Chlamydomonas reinhardtii-An Enzyme Involved in the Photosynthetic Calvin-Benson Cycle.,Le Moigne T, Crozet P, Lemaire SD, Henri J Int J Mol Sci. 2020 Oct 21;21(20). pii: ijms21207787. doi: 10.3390/ijms21207787. PMID:33096784<ref>PMID:33096784</ref>

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

==See Also==
*[[Ribose-5-phosphate isomerase 3D structures|Ribose-5-phosphate isomerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydomonas reinhardtii]]
[[Category: Large Structures]]
[[Category: Crozet P]]
[[Category: Henri J]]
[[Category: Le Moigne T]]
[[Category: Lemaire SD]]