6zxt: Difference between revisions
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==High resolution crystal structure of chloroplastic ribose-5-phosphate isomerase from Chlamydomonas reinhardtii== | |||
<StructureSection load='6zxt' size='340' side='right'caption='[[6zxt]], [[Resolution|resolution]] 1.40Å' 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]] 1.4Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Crozet | <div class="pdbe-citations 6zxt" style="background-color:#fffaf0;"></div> | ||
[[Category: Henri | |||
[[Category: Le Moigne | ==See Also== | ||
[[Category: Lemaire | *[[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]] | |||
Latest revision as of 14:59, 1 February 2024
High resolution crystal structure of chloroplastic ribose-5-phosphate isomerase from Chlamydomonas reinhardtiiHigh resolution crystal structure of chloroplastic ribose-5-phosphate isomerase from Chlamydomonas reinhardtii
Structural highlights
FunctionPublication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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