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| | ==Crystal structure of limiting CO2-inducible protein LCIB== | | ==Crystal structure of limiting CO2-inducible protein LCIB== |
| - | <StructureSection load='5k5w' size='340' side='right' caption='[[5k5w]], [[Resolution|resolution]] 2.59Å' scene=''> | + | <StructureSection load='5k5w' size='340' side='right'caption='[[5k5w]], [[Resolution|resolution]] 2.59Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5k5w]] is a 2 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=5K5W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5K5W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5k5w]] 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=5K5W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5K5W FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 2.591Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b5x|5b5x]], [[5b5y|5b5y]], [[5b5z|5b5z]], [[5b60|5b60]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pmp1, LCIB ([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'>[https://proteopedia.org/fgij/fg.htm?mol=5k5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k5w OCA], [https://pdbe.org/5k5w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5k5w RCSB], [https://www.ebi.ac.uk/pdbsum/5k5w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5k5w 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=5k5w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5k5w OCA], [http://pdbe.org/5k5w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5k5w RCSB], [http://www.ebi.ac.uk/pdbsum/5k5w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5k5w ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q0ZAI6_CHLRE Q0ZAI6_CHLRE] |
| | <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: Chlre]] | + | [[Category: Chlamydomonas reinhardtii]] |
| - | [[Category: Gao, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Jin, S]] | + | [[Category: Gao Y]] |
| - | [[Category: Mueller-Cajar, O M]] | + | [[Category: Jin S]] |
| - | [[Category: Sun, J]] | + | [[Category: Mueller-Cajar OM]] |
| - | [[Category: Tang, D]] | + | [[Category: Sun J]] |
| - | [[Category: Wunder, T]] | + | [[Category: Tang D]] |
| - | [[Category: Metal binding protein]]
| + | [[Category: Wunder T]] |
| - | [[Category: Metalloprotein]]
| + | |
| Structural highlights
Function
Q0ZAI6_CHLRE
Publication Abstract from PubMed
Aquatic microalgae have evolved diverse CO2-concentrating mechanisms (CCMs) to saturate the carboxylase with its substrate, to compensate for the slow kinetics and competing oxygenation reaction of the key photosynthetic CO2-fixing enzyme rubisco. The limiting CO2-inducible B protein (LCIB) is known to be essential for CCM function in Chlamydomonas reinhardtii To assign a function to this previously uncharacterized protein family, we purified and characterized a phylogenetically diverse set of LCIB homologs. Three of the six homologs are functional carbonic anhydrases (CAs). We determined the crystal structures of LCIB and limiting CO2-inducible C protein (LCIC) from C. reinhardtii and a CA-functional homolog from Phaeodactylum tricornutum, all of which harbor motifs bearing close resemblance to the active site of canonical beta-CAs. Our results identify the LCIB family as a previously unidentified group of beta-CAs, and provide a biochemical foundation for their function in the microalgal CCMs.
Structural insights into the LCIB protein family reveals a new group of beta-carbonic anhydrases.,Jin S, Sun J, Wunder T, Tang D, Cousins AB, Sze SK, Mueller-Cajar O, Gao YG Proc Natl Acad Sci U S A. 2016 Dec 20;113(51):14716-14721. doi:, 10.1073/pnas.1616294113. Epub 2016 Dec 1. PMID:27911826[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jin S, Sun J, Wunder T, Tang D, Cousins AB, Sze SK, Mueller-Cajar O, Gao YG. Structural insights into the LCIB protein family reveals a new group of beta-carbonic anhydrases. Proc Natl Acad Sci U S A. 2016 Dec 20;113(51):14716-14721. doi:, 10.1073/pnas.1616294113. Epub 2016 Dec 1. PMID:27911826 doi:http://dx.doi.org/10.1073/pnas.1616294113
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