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| | ==Structure and identification of a pterin dehydratase-like protein as a RuBisCO assembly factor in the alpha-carboxysome== | | ==Structure and identification of a pterin dehydratase-like protein as a RuBisCO assembly factor in the alpha-carboxysome== |
| - | <StructureSection load='4low' size='340' side='right' caption='[[4low]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='4low' size='340' side='right'caption='[[4low]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4low]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thik1 Thik1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LOW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LOW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4low]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thiomonas_intermedia_K12 Thiomonas intermedia K12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LOW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tint_0125 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=75379 THIK1])</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=4low FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4low OCA], [https://pdbe.org/4low PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4low RCSB], [https://www.ebi.ac.uk/pdbsum/4low PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4low ProSAT]</span></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=4low FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4low OCA], [http://pdbe.org/4low PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4low RCSB], [http://www.ebi.ac.uk/pdbsum/4low PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4low ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D5X340_THIK1 D5X340_THIK1] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Thik1]] | + | [[Category: Large Structures]] |
| - | [[Category: Cascio, D]] | + | [[Category: Thiomonas intermedia K12]] |
| - | [[Category: Gidaniyan, S D]] | + | [[Category: Cascio D]] |
| - | [[Category: Wheatley, N M]] | + | [[Category: Gidaniyan SD]] |
| - | [[Category: Yeates, T O]] | + | [[Category: Wheatley NM]] |
| - | [[Category: Pcd]] | + | [[Category: Yeates TO]] |
| - | [[Category: Pterin-4a-carbinolamine dehydratase-like]]
| + | |
| - | [[Category: Unknown function]]
| + | |
| Structural highlights
Function
D5X340_THIK1
Publication Abstract from PubMed
Carboxysomes are proteinaceous bacterial microcompartments that increase the efficiency of the rate-limiting step in carbon fixation by sequestering reaction substrates. Typically, alpha-carboxysomes are genetically encoded as a single operon expressing the microcompartment's structural proteins and its encapsulated enzymes. In addition, depending on phylogeny, as many as thirteen other genes are found to co-occur near or within alpha-carboxysome operons. One of these genes codes for a protein with distant homology to pterin-4a-carbinolamine dehydratase (PCD) enzymes. It is present in all alpha-carboxysome containing bacteria and has homologs in algae and higher plants. Canonical PCDs play an important role in amino acid hydroxylation, a reaction not associated with carbon fixation. We determined the crystal structure of an alpha-carboxysome PCD-like protein from the chemoautotrophic bacterium Thiomonas intermedia K12, at a resolution of 1.3 A. The protein retains a three-dimensional fold similar to canonical PCDs, though the prominent active site cleft present in PCD enzymes is disrupted in the alpha-carboxysome PCD-like protein. Using a cell-based complementation assay, we tested the PCD-like proteins from T. intermedia and two additional bacteria, and found no evidence for PCD enzymatic activity. However, we discovered that heterologous co-expression of the PCD-like protein from H. neapolitanus with RuBisCO and GroELS in E. coli increased the amount of soluble, assembled RuBisCO recovered from cell lysates compared to co-expression of RuBisCO with GroELS alone. We conclude that this conserved PCD-like protein, renamed here alpha carboxysome RuBisCO assembly factor (or acRAF), is a novel RuBisCO chaperone integral to alpha-carboxysome function.
Structure and identification of a pterin dehydratase-like protein as a RuBisCO assembly factor in the alpha-carboxysome.,Wheatley NM, Sundberg CD, Gidaniyan SD, Cascio D, Yeates TO J Biol Chem. 2014 Jan 23. PMID:24459150[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wheatley NM, Sundberg CD, Gidaniyan SD, Cascio D, Yeates TO. Structure and identification of a pterin dehydratase-like protein as a RuBisCO assembly factor in the alpha-carboxysome. J Biol Chem. 2014 Jan 23. PMID:24459150 doi:http://dx.doi.org/10.1074/jbc.M113.531236
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