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TitleStructural and functional analysis of a photosystem II mutant PsbA3-S264V.
Journal, issue, pagesBiochim Biophys Acta Bioenerg, Vol. 1868, Issue 1, Page 149607, Year 2026
Publish dateSep 6, 2026
AuthorsSongbo Fan / Yoshiki Nakajima / Koji Kato / Haowei Jiang / Pi-Cheng Tsai / Anqi Jia / Miwa Sugiura / Jian-Ren Shen /
PubMed AbstractPhotosystem II (PSII) catalyzes water oxidation and oxygen evolution by a light-induced electron transfer chain, leading to the generation of electrons, protons and dioxygen. D1-S264 is a residue ...Photosystem II (PSII) catalyzes water oxidation and oxygen evolution by a light-induced electron transfer chain, leading to the generation of electrons, protons and dioxygen. D1-S264 is a residue located close to the Q-binding site, and mutation of this residue has been shown to bring significant effects on the electron transfer and oxygen-evolving activities. Here we analyzed the structure of a Thermosynechococcus elongatus mutant PsbA3-S264V by cryo-electron microscopy at 1.96 Å resolution, which showed significant changes in the structure surrounding the bicarbonate and Q-binding region. Due to change of Ser to Val, the hydrogen-bond between the Q carbonyl oxygen and S264 is altered, which changed the protonation pathway of Q from the original route of D1-H252 through D1-S264 to Q, to a new, longer and less efficient route of D1-H252 through D1-F265 to Q. Two residues, D1-E244 and D2-E242, changed their side chain orientations significantly. Among them, D2-E242 adopted two conformations, and both are largely deviated from the original structure. All these changes led to alterations in hydrogen-bonding networks of two channels, channel A and channel B, that connect the stromal surface to Q and may function to transport protons to protonate Q. Furthermore, isothermal titration calorimetry experiments showed a diminished 3-(3,4-dichlorophenyl)-1, 1-dimethylurea (DCMU) binding affinity of the mutated PSII, which may be explained by a structural rotation of D1-F255 in the mutant based on structural analysis of DCMU-bound PSII. These findings offer valuable insights into the functions of D1-S264 in Q protonation and function, as well as in the DCMU-binding.
External linksBiochim Biophys Acta Bioenerg / PubMed:42702229
MethodsEM (single particle)
Resolution1.96 - 2.08 Å
Structure data

65652

9w5b

EMDB-65652, PDB-9w5b:
cryo-EM structure of PSII D1-S264V from Thermosynechococcus vestitus BP-1
Method: EM (single particle) / Resolution: 1.96 Å

65724

9w7d

EMDB-65724, PDB-9w7d:
cryo-EM structure of PSII PsbA3-S264V in complex with DCMU from Thermosynechococcus vestitus BP-1
Method: EM (single particle) / Resolution: 2.05 Å

65941

9wfz

EMDB-65941, PDB-9wfz:
Cryo-EM structure of PSII PsbA3-S264V from Thermosynechococcus vestitus BP-1 (local refinement)
Method: EM (single particle) / Resolution: 2.08 Å

Chemicals

ChemComp-OEX:
CA-MN4-O5 CLUSTER

ChemComp-FE2:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-CLA:
CHLOROPHYLL A

ChemComp-BCR:
BETA-CAROTENE

ChemComp-SQD:
1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-GLUCOPYRANOSYL]-SN-GLYCEROL

ChemComp-PL9:
2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-BENZOQUINONE


ChemComp, No image

ChemComp-UNL:
Unknown ligand

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

ChemComp-LHG:
1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE / phospholipid*YM

ChemComp-LMG:
1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

ChemComp-DGD:
DIGALACTOSYL DIACYL GLYCEROL (DGDG)

ChemComp-PHO:
PHEOPHYTIN A

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-CA:
Unknown entry

ChemComp-HEC:
HEME C

ChemComp-RRX:
(3R)-beta,beta-caroten-3-ol

ChemComp-HOH:
WATER

ChemComp-W9M:
3-(3,4-dichlorophenyl)-1,1-dimethyl-urea

Source
  • thermosynechococcus vestitus bp-1 (bacteria)
KeywordsPHOTOSYNTHESIS / PSII mutation / DCMU / local refinement

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