Structural and functional studies of low-CO2 inducible protein LCIB homolog from phaeodactylumtricornutuminvolved in CO2-concentrating mechanism

Global warming and food crisis urge us to improve global productivity. However, photosynthesis is limited by poor efficiency and specificity of Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Many organisms develop CO2-concentrating mechanisms (CCMs) to maintain high CO2 concentration nea...

Full description

Bibliographic Details
Main Author: Luo, Yuanyuan
Other Authors: Gao Yonggui
Format: Final Year Project (FYP)
Language:English
Published: 2017
Subjects:
Online Access:http://hdl.handle.net/10356/70763
_version_ 1826123482710147072
author Luo, Yuanyuan
author2 Gao Yonggui
author_facet Gao Yonggui
Luo, Yuanyuan
author_sort Luo, Yuanyuan
collection NTU
description Global warming and food crisis urge us to improve global productivity. However, photosynthesis is limited by poor efficiency and specificity of Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Many organisms develop CO2-concentrating mechanisms (CCMs) to maintain high CO2 concentration near Rubisco. The low-CO2 inducible B protein (LCIB) in Chlamydomonasreinhardtii was found to bear close structural resemblance to classic beta-type carbonic anhydrase (CA) which plays an important role in CCM. Its homolog in diatom PhaeodactylumtricornutumPtLCIB4 showed significantly increased CA activity with addition of Copper ion. With the aim to study the influence of Cu2+ on its structure and function, PtLCIB4 was expressed as a recombinant protein in E.coli and purified by nickel affinity chromatography and size exclusion chromatography. Crystallization screening was performed on the purified protein which was further co-crystallized and soaked with CuCl2. The crystal structure of PtLCIB4-Cu was obtained by X-ray diffraction with resolution up to 2 Å. No significant difference was observed after superimposing its crystal structure with copper-freePtLCIB4. Thus, hypothesis of facile metal ion exchange between copper and zinc in the active site of PtLCIB4 was proposed which need to be verified by fluorescence scanning at synchrotron radiation facility. Remove
first_indexed 2024-10-01T06:05:22Z
format Final Year Project (FYP)
id ntu-10356/70763
institution Nanyang Technological University
language English
last_indexed 2024-10-01T06:05:22Z
publishDate 2017
record_format dspace
spelling ntu-10356/707632023-02-28T18:06:05Z Structural and functional studies of low-CO2 inducible protein LCIB homolog from phaeodactylumtricornutuminvolved in CO2-concentrating mechanism Luo, Yuanyuan Gao Yonggui School of Biological Sciences Institute of Structural Biology DRNTU::Science::Biological sciences Global warming and food crisis urge us to improve global productivity. However, photosynthesis is limited by poor efficiency and specificity of Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco). Many organisms develop CO2-concentrating mechanisms (CCMs) to maintain high CO2 concentration near Rubisco. The low-CO2 inducible B protein (LCIB) in Chlamydomonasreinhardtii was found to bear close structural resemblance to classic beta-type carbonic anhydrase (CA) which plays an important role in CCM. Its homolog in diatom PhaeodactylumtricornutumPtLCIB4 showed significantly increased CA activity with addition of Copper ion. With the aim to study the influence of Cu2+ on its structure and function, PtLCIB4 was expressed as a recombinant protein in E.coli and purified by nickel affinity chromatography and size exclusion chromatography. Crystallization screening was performed on the purified protein which was further co-crystallized and soaked with CuCl2. The crystal structure of PtLCIB4-Cu was obtained by X-ray diffraction with resolution up to 2 Å. No significant difference was observed after superimposing its crystal structure with copper-freePtLCIB4. Thus, hypothesis of facile metal ion exchange between copper and zinc in the active site of PtLCIB4 was proposed which need to be verified by fluorescence scanning at synchrotron radiation facility. Remove Bachelor of Science in Biological Sciences 2017-05-11T04:33:47Z 2017-05-11T04:33:47Z 2017 Final Year Project (FYP) http://hdl.handle.net/10356/70763 en Nanyang Technological University 30 p. application/pdf
spellingShingle DRNTU::Science::Biological sciences
Luo, Yuanyuan
Structural and functional studies of low-CO2 inducible protein LCIB homolog from phaeodactylumtricornutuminvolved in CO2-concentrating mechanism
title Structural and functional studies of low-CO2 inducible protein LCIB homolog from phaeodactylumtricornutuminvolved in CO2-concentrating mechanism
title_full Structural and functional studies of low-CO2 inducible protein LCIB homolog from phaeodactylumtricornutuminvolved in CO2-concentrating mechanism
title_fullStr Structural and functional studies of low-CO2 inducible protein LCIB homolog from phaeodactylumtricornutuminvolved in CO2-concentrating mechanism
title_full_unstemmed Structural and functional studies of low-CO2 inducible protein LCIB homolog from phaeodactylumtricornutuminvolved in CO2-concentrating mechanism
title_short Structural and functional studies of low-CO2 inducible protein LCIB homolog from phaeodactylumtricornutuminvolved in CO2-concentrating mechanism
title_sort structural and functional studies of low co2 inducible protein lcib homolog from phaeodactylumtricornutuminvolved in co2 concentrating mechanism
topic DRNTU::Science::Biological sciences
url http://hdl.handle.net/10356/70763
work_keys_str_mv AT luoyuanyuan structuralandfunctionalstudiesoflowco2inducibleproteinlcibhomologfromphaeodactylumtricornutuminvolvedinco2concentratingmechanism