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6TJV

Structure of the NDH-1MS complex from Thermosynechococcus elongatus

Summary for 6TJV
Entry DOI10.2210/pdb6tjv/pdb
EMDB information10513
DescriptorNAD(P)H-quinone oxidoreductase subunit 1, NAD(P)H-quinone oxidoreductase subunit J, NAD(P)H-quinone oxidoreductase subunit K, ... (26 entities in total)
Functional Keywordscarbon concentrating photosynthetic complex i, proton pump, membrane protein
Biological sourceThermosynechococcus elongatus (strain BP-1)
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Total number of polymer chains18
Total formula weight511378.09
Authors
Schuller, J.M.,Saura, P.,Thiemann, J.,Schuller, S.K.,Gamiz-Hernandez, A.P.,Kurisu, G.,Nowaczyk, M.M.,Kaila, V.R.I. (deposition date: 2019-11-27, release date: 2020-02-19, Last modification date: 2025-10-01)
Primary citationSchuller, J.M.,Saura, P.,Thiemann, J.,Schuller, S.K.,Gamiz-Hernandez, A.P.,Kurisu, G.,Nowaczyk, M.M.,Kaila, V.R.I.
Redox-coupled proton pumping drives carbon concentration in the photosynthetic complex I.
Nat Commun, 11:494-494, 2020
Cited by
PubMed Abstract: Photosynthetic organisms capture light energy to drive their energy metabolism, and employ the chemical reducing power to convert carbon dioxide (CO) into organic molecules. Photorespiration, however, significantly reduces the photosynthetic yields. To survive under low CO concentrations, cyanobacteria evolved unique carbon-concentration mechanisms that enhance the efficiency of photosynthetic CO fixation, for which the molecular principles have remained unknown. We show here how modular adaptations enabled the cyanobacterial photosynthetic complex I to concentrate CO using a redox-driven proton-pumping machinery. Our cryo-electron microscopy structure at 3.2 Å resolution shows a catalytic carbonic anhydrase module that harbours a Zn active site, with connectivity to proton-pumping subunits that are activated by electron transfer from photosystem I. Our findings illustrate molecular principles in the photosynthetic complex I machinery that enabled cyanobacteria to survive in drastically changing CO conditions.
PubMed: 31980611
DOI: 10.1038/s41467-020-14347-4
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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