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TitleCryo-EM structure of photosystem II D1-V185T mutant from Thermosynechococcus vestitus.
Journal, issue, pagesBiochim Biophys Acta Bioenerg, Vol. 1867, Issue 4, Page 149598, Year 2026
Publish dateJun 22, 2026
AuthorsHaowei Jiang / Yoshiki Nakajima / Fusamichi Akita / Hongjie Li / Koji Kato / Miwa Sugiura / Jian-Ren Shen /
PubMed AbstractPhotosystem II (PSII) catalyzes water oxidation into electrons, protons and dioxygen at its catalytic center, a MnCaO cluster, utilizing light energy. An amino acid residue D1-V185 in the D1 protein ...Photosystem II (PSII) catalyzes water oxidation into electrons, protons and dioxygen at its catalytic center, a MnCaO cluster, utilizing light energy. An amino acid residue D1-V185 in the D1 protein is located close to the MnCaO cluster, and plays a critical role in its catalytic function. In this research we purified PSII dimers from a D1-V185T mutant of Thermosynechococcus vestitus and analyzed its structure using low-damage cryo-electron microscopy (cryo-EM) at a resolution of 1.88 Å. The results revealed the presence of multi-conformations at the mutation site. Unlike the wild-type valine, which does not allow water molecules to be able to form hydrogen-bonds with it, both conformations of the mutant formed hydrogen bonds with nearby water molecules, which leads to rearrangement of the hydrogen bond networks in the O1 and Cl-1 channels. In conformation-A, the mutated Thr residue forms a hydrogen bond with a water molecule W6, which creates a new channel that bypasses the original O1 channel. Due to the hydrophilic OH group of Thr, the side-chain of D1-Glu189 was attracted and shifted toward the mutant Thr residue. In conformation-B, it forms a hydrogen bond with a water molecule W9 in the Cl-1 channel, bringing W9 closer and thereby disrupting the hydrogen bond network of the Cl-1 channel. In addition, multi-conformations of D2-K317, which is a ligand of Cl-1, were found in the mutant. These changes alter the environment surrounding the Cl-1 ion and MnCaO, thereby affecting the PSII water-oxidation activity.
External linksBiochim Biophys Acta Bioenerg / PubMed:42331212
MethodsEM (single particle)
Resolution1.88 Å
Structure data

63639

9m5a

EMDB-63639, PDB-9m5a:
cryo-EM structure of PSII D1-V185T from Thermosynechococcus vestitus BP-1
Method: EM (single particle) / Resolution: 1.88 Å

Chemicals

ChemComp-OEX:
CA-MN4-O5 CLUSTER

ChemComp-FE2:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-CLA:
CHLOROPHYLL A

ChemComp-PHO:
PHEOPHYTIN A

ChemComp-BCR:
BETA-CAROTENE

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

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


ChemComp, No image

ChemComp-UNL:
Unknown ligand

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

ChemComp-DGD:
DIGALACTOSYL DIACYL GLYCEROL (DGDG)

ChemComp-BCT:
BICARBONATE ION

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

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

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

ChemComp-MG:
Unknown entry

ChemComp-HEC:
HEME C

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • Thermosynechococcus vestitus (bacteria)
  • thermosynechococcus vestitus bp-1 (bacteria)
KeywordsPHOTOSYNTHESIS / PSII mutation

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