ISDA: 6ZOO

Deposition Date 2020-07-07

Release Date 2021-06-16

Last Version Date 2026-09-16

Entry Detail

PDB ID:

6ZOO

Keywords:

PHOTOSYNTHESIS

Title:

Photosystem I reduced Plastocyanin Complex

Biological Source:

Source Organism(s):

Pisum sativum (Taxon ID: 3888)

Method Details:

Experimental Method:

ELECTRON MICROSCOPY

Resolution:

2.74 Å

Aggregation State:

PARTICLE

Reconstruction Method:

SINGLE PARTICLE

Download Validation Report

Macromolecular Entities

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Chlorophyll a-b binding prote
Gene (Uniprot):LHCA1
Chain IDs:M (auth: 1)
Chain Length:193
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:Q01667 Pfam ID:PF00504

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Chlorophyll a-b binding prote
Gene (Uniprot):lhaB
Chain IDs:N (auth: 2)
Chain Length:208
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:Q41038 Pfam ID:PF00504

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Chlorophyll a-b binding prote
Gene (Uniprot):lhca3
Chain IDs:O (auth: 3)
Chain Length:221
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:Q32904 Pfam ID:PF00504

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Chlorophyll a-b binding prote
Gene (Uniprot):lhcA-P4
Chain IDs:P (auth: 4)
Chain Length:198
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:Q9SQL2 Pfam ID:PF00504

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Photosystem I P700 chlorophyl
Gene (Uniprot):psaA
Chain IDs:A
Chain Length:743
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:A0A0F6NFW5 Pfam ID:PF00223 EC:1.97.1.12

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Photosystem I P700 chlorophyl
Gene (Uniprot):psaB
Chain IDs:B
Chain Length:733
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:A0A0F6NGI2 Pfam ID:PF00223 EC:1.97.1.12

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Photosystem I iron-sulfur cen
Gene (Uniprot):psaC
Chain IDs:C
Chain Length:80
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:P10793 Pfam ID:PF14697 EC:1.97.1.12

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:PsaD
Chain IDs:D
Chain Length:143
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:E1C9K8 Pfam ID:PF02531

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Putative uncharacterized prot
Chain IDs:E
Chain Length:66
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:E1C9K6 Pfam ID:PF02427

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Chain IDs:F
Chain Length:154
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:A0A0M3KL12 Pfam ID:PF02507

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:photosystem I reaction center
Chain IDs:G
Chain Length:97
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:A0A0M3KL13 Pfam ID:PF01241

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Chain IDs:H
Chain Length:93
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:A0A0M3KL10,P20121 Pfam ID:PF03244

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):psaI
Chain IDs:I
Chain Length:31
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:P17227 Pfam ID:PF00796 EC:1.97.1.12

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Gene (Uniprot):psaJ
Chain IDs:J
Chain Length:42
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:D5MAL3 Pfam ID:PF01701

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Photosystem I reaction center
Chain IDs:K
Chain Length:81
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:E1C9L3 Pfam ID:PF01241

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:PsaL domain-containing protei
Chain IDs:L
Chain Length:159
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:E1C9L1 Pfam ID:PF02605

Structures with similar UniProt ID

Structural Superimposition Protein Blast

Polymer Type:polypeptide(L)
Molecule:Plastocyanin, chloroplastic
Gene (Uniprot):PETE
Chain IDs:Q (auth: P)
Chain Length:99
Number of Molecules:1
Biological Source:Pisum sativum

UniProt ID:P16002 Pfam ID:PF00127

Modified Residue

Compound ID	Chain ID	Parent Comp ID	Details	2D Image
SNK	A	HIS	modified residue

Ligand Molecules

3PH

BCR

CHL

CL0

CLA

DGD

LHG

LMG

LMT

LUT

PQN

SF4

XAT

Primary Citation

Structure of plant photosystem I-plastocyanin complex reveals strong hydrophobic interactions.

Caspy, I, Fadeeva, M, Kuhlgert, S, Borovikova-Sheinker, A, Klaiman, D, Masrati, G, Drepper, F, Ben-Tal, N, Hippler, M, Nelson, N.Show

Biochem.J. 478 2371 2384 (2021)

PMID: 34085703 DOI: 10.1042/BCJ20210267

Abstact

Photosystem I is defined as plastocyanin-ferredoxin oxidoreductase. Taking advantage of genetic engineering, kinetic analyses and cryo-EM, our data provide novel mechanistic insights into binding and electron transfer between PSI and Pc. Structural data at 2.74 Å resolution reveals strong hydrophobic interactions in the plant PSI-Pc ternary complex, leading to exclusion of water molecules from PsaA-PsaB/Pc interface once the PSI-Pc complex forms. Upon oxidation of Pc, a slight tilt of bound oxidized Pc allows water molecules to accommodate the space between Pc and PSI to drive Pc dissociation. Such a scenario is consistent with the six times larger dissociation constant of oxidized as compared with reduced Pc and mechanistically explains how this molecular machine optimized electron transfer for fast turnover.

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Protein

Chemical

Disease

Primary Citation of related structures

Abstact

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