This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4low
From Proteopedia
(Difference between revisions)
| Line 4: | Line 4: | ||
== Structural highlights == | == Structural highlights == | ||
<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> | <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" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</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='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'>[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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/D5X340_THIK1 D5X340_THIK1] | [https://www.uniprot.org/uniprot/D5X340_THIK1 D5X340_THIK1] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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<ref>PMID:24459150</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4low" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure and identification of a pterin dehydratase-like protein as a RuBisCO assembly factor in the alpha-carboxysome
| |||||||||||
