Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases
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...
| Autori principali: | , , , , , , , |
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| Natura: | Journal Article |
| Lingua: | English |
| Pubblicazione: |
2017
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| Accesso online: | https://hdl.handle.net/10356/85138 http://hdl.handle.net/10220/43642 |
| _version_ | 1826122913844035584 |
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| author | Jin, Shengyang Sun, Jian Wunder, Tobias Tang, Desong Cousins, Asaph B. Sze, Siu Kwan Mueller-Cajar, Oliver Gao, Yong-Gui |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Jin, Shengyang Sun, Jian Wunder, Tobias Tang, Desong Cousins, Asaph B. Sze, Siu Kwan Mueller-Cajar, Oliver Gao, Yong-Gui |
| author_sort | Jin, Shengyang |
| collection | NTU |
| description | 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. |
| first_indexed | 2024-10-01T05:56:03Z |
| format | Journal Article |
| id | ntu-10356/85138 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T05:56:03Z |
| publishDate | 2017 |
| record_format | dspace |
| spelling | ntu-10356/851382023-02-28T16:59:58Z Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases Jin, Shengyang Sun, Jian Wunder, Tobias Tang, Desong Cousins, Asaph B. Sze, Siu Kwan Mueller-Cajar, Oliver Gao, Yong-Gui School of Biological Sciences Limiting-CO2 inducible protein LCIB 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. NRF (Natl Research Foundation, S’pore) MOE (Min. of Education, S’pore) Accepted version 2017-08-28T09:26:19Z 2019-12-06T15:57:54Z 2017-08-28T09:26:19Z 2019-12-06T15:57:54Z 2016 Journal Article 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. 0027-8424 https://hdl.handle.net/10356/85138 http://hdl.handle.net/10220/43642 10.1073/pnas.1616294113 en Proceedings of the National Academy of Sciences of the United States of America © 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]. 26 p. application/pdf |
| spellingShingle | Limiting-CO2 inducible protein LCIB Jin, Shengyang Sun, Jian Wunder, Tobias Tang, Desong Cousins, Asaph B. Sze, Siu Kwan Mueller-Cajar, Oliver Gao, Yong-Gui Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases |
| title | Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases |
| title_full | Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases |
| title_fullStr | Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases |
| title_full_unstemmed | Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases |
| title_short | Structural insights into the LCIB protein family reveals a new group of β-carbonic anhydrases |
| title_sort | structural insights into the lcib protein family reveals a new group of β carbonic anhydrases |
| topic | Limiting-CO2 inducible protein LCIB |
| url | https://hdl.handle.net/10356/85138 http://hdl.handle.net/10220/43642 |
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