5b5z

Crystal structure of PtLCIB4 H88A mutant, a homolog of the limiting CO2-inducible protein LCIB

spinqualitylabelsall models 5b5z, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5b5z is a 2 chain structure with sequence from Phaeodactylum tricornutum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B7FR29_PHATC 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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