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Structure of the undecorated barbed end of F-actin.
Resolution: 3.08 Å
EM Method: Single-particle
Fitted PDBs: 8ru0
Q-score: 0.542
Oosterheert W, Boiero Sanders M, Funk J, Prumbaum D, Raunser S, Bieling P
Science (2024) 384 pp. eadn9560-eadn9560 [ DOI: doi:10.1126/science.adn9560 Pubmed: 38603491 ]
- Phosphate ion (94 Da, Ligand)
- Adenosine-5'-diphosphate (427 Da, Ligand)
- Actin, alpha skeletal muscle (41 kDa, Protein from Oryctolagus cuniculus)
- Adenosine-5'-triphosphate (507 Da, Ligand)
- Actin filament (Complex)
- Magnesium ion (24 Da, Ligand)
- Complex of the actin subunits that form the barbed end of actin filaments. (Complex from Oryctolagus cuniculus)
Structure of the formin INF2 bound to the barbed end of F-actin.
Resolution: 3.41 Å
EM Method: Single-particle
Fitted PDBs: 8rv2
Q-score: 0.43
Oosterheert W, Boiero Sanders M, Funk J, Prumbaum D, Raunser S, Bieling P
Science (2024) 384 pp. eadn9560-eadn9560 [ DOI: doi:10.1126/science.adn9560 Pubmed: 38603491 ]
- Inf2 dimer (Complex from Homo sapiens)
- Phosphate ion (94 Da, Ligand)
- Actin filament barbed end (Complex from Oryctolagus cuniculus)
- Adenosine-5'-diphosphate (427 Da, Ligand)
- Actin, alpha skeletal muscle (41 kDa, Protein from Oryctolagus cuniculus)
- Adenosine-5'-triphosphate (507 Da, Ligand)
- Isoform 2 of inverted formin-2 (84 kDa, Protein from Homo sapiens)
- Complex of the formin inf2 dimer that binds to the actin subunits at the barbed end of actin filaments. (Complex)
- Magnesium ion (24 Da, Ligand)
Cryo-EM structure of Myosin VI in the autoinhibited state (without SAH-extension density)
Resolution: 3.54 Å
EM Method: Single-particle
Fitted PDBs: 8w41
Q-score: 0.34
Niu F, Li L, Wang L, Xiao J, Xu S, Liu Y, Lin L, Yu C, Wei Z
Nat Commun (2024) 15 pp. 1187-1187 [ DOI: doi:10.1038/s41467-024-45424-7 Pubmed: 38331992 ]
- Complex of myosin vi and calmodulin (Complex)
- Phosphate ion (94 Da, Ligand)
- Myosin vi (Complex from Homo sapiens)
- Adenosine-5'-diphosphate (427 Da, Ligand)
- Calmodulin (Complex from Mus musculus)
- Magnesium ion (24 Da, Ligand)
- Calmodulin-1 (16 kDa, Protein from Mus musculus)
- Unconventional myosin-vi (148 kDa, Protein from Homo sapiens)
- Calcium ion (40 Da, Ligand)
Cryo-EM map of Myosin VI in the autoinhibited state (with SAH-extension density)
Niu F, Li L, Wang L, Xiao J, Xu S, Liu Y, Lin L, Yu C, Wei Z
Nat Commun (2024) 15 pp. 1187-1187 [ DOI: doi:10.1038/s41467-024-45424-7 Pubmed: 38331992 ]
- Myosin vi (Complex from Homo sapiens)
- Complex of myosin vi and calmodulin (Complex)
- Myosin vi (Protein from Homo sapiens)
- Calmodulin (Complex from Mus musculus)
- Calmodulin (Protein from Mus musculus)
The structure of the PP2A-B56Delta holoenzyme mutant - E197K
Resolution: 2.7 Å
EM Method: Single-particle
Fitted PDBs: 8u1x
Q-score: 0.556
Wu CG, Balakrishnan VK, Merrill RA, Parihar PS, Konovolov K, Chen YC, Xu Z, Wei H, Sundaresan R, Cui Q, Wadzinski BE, Swingle MR, Musiyenko A, Chung WK, Honkanen RE, Suzuki A, Huang X, Strack S, Xing Y
PNAS (2024) 121 pp. e2310727120-e2310727120 [ Pubmed: 38150499 DOI: doi:10.1073/pnas.2310727120 ]
- Serine/threonine-protein phosphatase 2a 56 kda regulatory subunit delta isoform (70 kDa, Protein from Homo sapiens)
- Manganese (ii) ion (54 Da, Ligand)
- Serine/threonine-protein phosphatase 2a 65 kda regulatory subunit a alpha isoform (65 kDa, Protein from Homo sapiens)
- Serine/threonine-protein phosphatase 2a catalytic subunit alpha isoform (35 kDa, Protein from Homo sapiens)
- Protein phosphatase 2a b56 delta holoenzyme mutant - e197k (Complex from Homo sapiens)
The structure of the PP2A-B56Delta holoenzyme mutant - E197K
Resolution: 3.3 Å
EM Method: Single-particle
Fitted PDBs: 8u89
Q-score: 0.447
Wu CG, Balakrishnan VK, Merrill RA, Parihar PS, Konovolov K, Chen YC, Xu Z, Wei H, Sundaresan R, Cui Q, Wadzinski BE, Swingle MR, Musiyenko A, Chung WK, Honkanen RE, Suzuki A, Huang X, Strack S, Xing Y
PNAS (2024) 121 pp. e2310727120-e2310727120 [ Pubmed: 38150499 DOI: doi:10.1073/pnas.2310727120 ]
- Serine/threonine-protein phosphatase 2a 56 kda regulatory subunit delta isoform (70 kDa, Protein from Homo sapiens)
- Manganese (ii) ion (54 Da, Ligand)
- Serine/threonine-protein phosphatase 2a 65 kda regulatory subunit a alpha isoform (65 kDa, Protein from Homo sapiens)
- Serine/threonine-protein phosphatase 2a catalytic subunit alpha isoform (35 kDa, Protein from Homo sapiens)
- Protein phosphatase 2a b56 delta holoenzyme mutant - e197k (Complex from Homo sapiens)
Atomic structure of Salmonella SipA/F-actin complex by cryo-EM
Resolution: 3.2 Å
EM Method: Helical reconstruction
Fitted PDBs: 8uee
Q-score: 0.506
Niedzialkowska E, Runyan L, Kudryashova E, Kudryashov DS, Egelman EH
To Be Published
- Cell invasion protein sipa (28 kDa, Protein from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2)
- Phosphate ion (94 Da, Ligand)
- Adenosine-5'-diphosphate (427 Da, Ligand)
- Actin, alpha skeletal muscle (41 kDa, Protein from Oryctolagus cuniculus)
- Sipa (Complex)
- Magnesium ion (24 Da, Ligand)
- Water (18 Da, Ligand)
- Actin, alpha skeletal muscle (Complex)
- Salmonella sipa/f-actin complex (Complex from Oryctolagus cuniculus)
Cryo-EM structure of the human cardiac myosin filament
Resolution: 6.4 Å
EM Method: Single-particle
Fitted PDBs: 8g4l
Q-score: 0.079
Dutta D, Nguyen V, Campbell KS, Padron R, Craig R
Nature (2023) 623 pp. 853-862 [ DOI: doi:10.1038/s41586-023-06691-4 Pubmed: 37914935 ]
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform (18 kDa, Protein from Homo sapiens)
- Myosin light chain 3 (21 kDa, Protein from Homo sapiens)
- Myosin filaments isolated from human cardiac left ventricular muscle (Tissue from Homo sapiens)
- Myosin-binding protein c, cardiac-type (140 kDa, Protein from Homo sapiens)
- Titin (119 kDa, Protein from Homo sapiens)
- Myosin-7 (223 kDa, Protein from Homo sapiens)
Cryo-EM structure of the human cardiac myosin filament
Dutta D, Nguyen V, Campbell KS, Padron R, Craig R
Nature (2023) 623 pp. 853-862 [ DOI: doi:10.1038/s41586-023-06691-4 Pubmed: 37914935 ]
Cryo-EM structure of the human cardiac myosin filament
Dutta D, Nguyen V, Campbell KS, Padron R, Craig R
Nature (2023) 623 pp. 853-862 [ DOI: doi:10.1038/s41586-023-06691-4 Pubmed: 37914935 ]