A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic. (Q33586572)

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English	A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic.	scientific article

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28154188%20AND%20SRC:MED&resulttype=core&format=json

9 April 2020

A unique structural domain in Methanococcoides burtonii ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) acts as a small subunit mimic (English)

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9 April 2020

Methanococcoides burtonii

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Methanococcoides burtonii

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1

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9 April 2020

Karin Valegård

2

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9 April 2020

Inger Andersson

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9 April 2020

author name string

Laura H Gunn

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28 July 2017

Karin Valegård

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28 July 2017

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30 January 2017

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9 April 2020

Journal of Biological Chemistry

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9 April 2020

292

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9 April 2020

16

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9 April 2020

6838-6850

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9 April 2020

describes a project that uses

1 reference

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A repeat protein links Rubisco to form the eukaryotic carbon-concentrating organelle

1 reference

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21 June 2018

Evolving Methanococcoides burtonii archaeal Rubisco for improved photosynthesis and plant growth

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Opposing effects of folding and assembly chaperones on evolvability of Rubisco

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21 June 2018

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1 reference

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Substrate-induced assembly of Methanococcoides burtonii D-ribulose-1,5-bisphosphate carboxylase/oxygenase dimers into decamers

1 reference

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Structural and functional similarities between a ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO)-like protein from Bacillus subtilis and photosynthetic RuBisCO.

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Rubisco regulation: a role for inhibitors

1 reference

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21 June 2018

New roads lead to Rubisco in archaebacteria

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COBALT: constraint-based alignment tool for multiple protein sequences

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Despite slow catalysis and confused substrate specificity, all ribulose bisphosphate carboxylases may be nearly perfectly optimized

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First crystal structure of Rubisco from a green alga, Chlamydomonas reinhardtii

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1 reference

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/28154188

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Perturbation of reaction-intermediate partitioning by a site-directed mutant of ribulose-bisphosphate carboxylase/oxygenase

1 reference

https://pubmed.ncbi.nlm.nih.gov/28154188

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based on heuristic

inferred from PubMed ID database lookup

Fallover of Ribulose 1,5-Bisphosphate Carboxylase/Oxygenase Activity : Decarbamylation of Catalytic Sites Depends on pH

1 reference

https://pubmed.ncbi.nlm.nih.gov/28154188

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Crystallographic analysis of ribulose 1,5-bisphosphate carboxylase from spinach at 2.4 A resolution. Subunit interactions and active site

1 reference

https://pubmed.ncbi.nlm.nih.gov/28154188

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based on heuristic

inferred from PubMed ID database lookup

Specificity for activase is changed by a Pro-89 to Arg substitution in the large subunit of ribulose-1,5-bisphosphate carboxylase/oxygenase

1 reference

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based on heuristic

inferred from PubMed ID database lookup

Two residues of rubisco activase involved in recognition of the Rubisco substrate

1 reference

https://pubmed.ncbi.nlm.nih.gov/28154188

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M116.767145

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28154188%20AND%20SRC:MED&resulttype=core&format=json

9 April 2020

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28154188%20AND%20SRC:MED&resulttype=core&format=json

9 April 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:28154188%20AND%20SRC:MED&resulttype=core&format=json

9 April 2020

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