5k5w
From Proteopedia
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<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> | <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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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. | ||
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| + | 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<ref>PMID:27911826</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5k5w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:08, 18 January 2017
Crystal structure of limiting CO2-inducible protein LCIB
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