|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5bs1' size='340' side='right'caption='[[5bs1]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='5bs1' size='340' side='right'caption='[[5bs1]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5bs1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Chlre Chlre]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BS1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BS1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5bs1]] is a 4 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=5BS1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BS1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5bs1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bs1 OCA], [https://pdbe.org/5bs1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bs1 RCSB], [https://www.ebi.ac.uk/pdbsum/5bs1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bs1 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CGL41, CHLREDRAFT_162607 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3055 CHLRE])</td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5bs1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bs1 OCA], [http://pdbe.org/5bs1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bs1 RCSB], [http://www.ebi.ac.uk/pdbsum/5bs1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5bs1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 22: |
Line 20: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chlre]] | + | [[Category: Chlamydomonas reinhardtii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bracher, A]] | + | [[Category: Bracher A]] |
| - | [[Category: Hartl, F U]] | + | [[Category: Hartl FU]] |
| - | [[Category: Hauser, T]] | + | [[Category: Hauser T]] |
| - | [[Category: Liu, C]] | + | [[Category: Liu C]] |
| - | [[Category: Mayer-Hartl, M]] | + | [[Category: Mayer-Hartl M]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Rbcx]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The most prevalent form of the Rubisco enzyme is a complex of eight catalytic large subunits (RbcL) and eight regulatory small subunits (RbcS). Rubisco biogenesis depends on the assistance by specific molecular chaperones. The assembly chaperone RbcX stabilizes the RbcL subunits after folding by chaperonin and mediates their assembly to the RbcL8 core complex, from which RbcX is displaced by RbcS to form active holoenzyme. Two isoforms of RbcX are found in eukaryotes, RbcX-I, which is more closely related to cyanobacterial RbcX, and the more distant RbcX-II. The green algae Chlamydomonas reinhardtii contains only RbcX-II isoforms, CrRbcX-IIa and CrRbcX-IIb. Here we solved the crystal structure of CrRbcX-IIa and show that it forms an arc-shaped dimer with a central hydrophobic cleft for binding the C-terminal sequence of RbcL. Like other RbcX proteins, CrRbcX-IIa supports the assembly of cyanobacterial Rubisco in vitro, albeit with reduced activity relative to cyanobacterial RbcX-I. Structural analysis of a fusion protein of CrRbcX-IIa and the C-terminal peptide of RbcL suggests that the peptide binding mode of RbcX-II may differ from that of cyanobacterial RbcX. RbcX homologs appear to have adapted to their cognate Rubisco clients as a result of co-evolution.
Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii.,Bracher A, Hauser T, Liu C, Hartl FU, Hayer-Hartl M PLoS One. 2015 Aug 25;10(8):e0135448. doi: 10.1371/journal.pone.0135448., eCollection 2015. PMID:26305355[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bracher A, Hauser T, Liu C, Hartl FU, Hayer-Hartl M. Structural Analysis of the Rubisco-Assembly Chaperone RbcX-II from Chlamydomonas reinhardtii. PLoS One. 2015 Aug 25;10(8):e0135448. doi: 10.1371/journal.pone.0135448., eCollection 2015. PMID:26305355 doi:http://dx.doi.org/10.1371/journal.pone.0135448
|
