Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/85138
Title: Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases
Authors: Jin, Shengyang
Sun, Jian
Wunder, Tobias
Tang, Desong
Cousins, Asaph B.
Sze, Siu Kwan
Mueller-Cajar, Oliver
Gao, Yong-Gui
Keywords: Limiting-CO2 inducible protein
LCIB
Issue Date: 2016
Source: Jin, S., Sun, J., Wunder, T., Tang, D., Cousins, A. B., Sze, S. K., et al. (2016). Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases. Proceedings of the National Academy of Sciences of the United States of America, 113(51), 14716-14721.
Series/Report no.: Proceedings of the National Academy of Sciences of the United States of America
Abstract: 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 β-CAs. Our results identify the LCIB family as a previously unidentified group of β-CAs, and provide a biochemical foundation for their function in the microalgal CCMs.
URI: https://hdl.handle.net/10356/85138
http://hdl.handle.net/10220/43642
ISSN: 0027-8424
DOI: 10.1073/pnas.1616294113
Rights: © 2016 The author(s) (published by National Academy of Sciences). This is the author created version of a work that has been peer reviewed and accepted for publication in Proceedings of the National Academy of Sciences of the United States of America, published by National Academy of Sciences on behalf of the author(s). It incorporates referee’s comments but changes resulting from the publishing process, such as copyediting, structural formatting, may not be reflected in this document.  The published version is available at: [http://dx.doi.org/10.1073/pnas.1616294113].
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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