Electron microscopy of the complex formed by chaperones TBCE and TBCB and alpha-tubulin
Serna M, Carranza G, Martin-Benito J, Janowski R, Canals A, Coll M, Zabala JC, Valpuesta JM
J Cell Sci (2015) 128 pp. 1824-1834 [ Pubmed: 25908846 DOI: doi:10.1242/jcs.167387 ]
- Alpha-tubulin (50 kDa, Protein from Bos taurus)
- Tubulin binding cofactor b (27 kDa, Protein from Homo sapiens)
- Tubulin binding cofactor e (59 kDa, Protein from Homo sapiens)
- Ternary complex of alpha-tubulin, tbce and tbcb (137 kDa, Sample)
Cryo-electron microscopy of T7 tail complex
Cuervo A, Pulido-Cid M, Chagoyen M, Arranz R, Gonzalez-Garcia VA, Garcia-Doval C, Caston JR, Valpuesta JM, van Raaij MJ, Martin-Benito J, Carrascosa JL
J Biol Chem (2013) 288 pp. 26290-26299 [ Pubmed: 23884409 DOI: doi:10.1074/jbc.M113.491209 ]
- Gp11 (25 kDa, Protein from Enterobacteria phage T7)
- Gp8 (59 kDa, Protein from Enterobacteria phage T7)
- T7 tail complex formed by proteins gp8, gp11, gp12, and gp17 (2 MDa, Sample)
- Gp12 (90 kDa, Protein from Enterobacteria phage T7)
- Gp17 (60 kDa, Protein from Enterobacteria phage T7)
Structural insights into the chaperone activity of Hsp40: DnaJ binds and remodels RepE
Cuellar J, Perales-Calvo J, Muga A, Valpuesta JM, Moro F
J Biol Chem (2013) 288 pp. 15065-15074 [ DOI: doi:10.1074/jbc.M112.430595 Pubmed: 23580641 ]
- Replication initiation factor of plasmid mini-f (60 kDa, Protein from Escherichia coli)
- Hsp40 (80 kDa, Protein from Escherichia coli)
- Dnaj:repe complex (140 kDa, Sample)
Structural insights into the chaperone activity of Hsp40: DnaJ binds and remodels RepE
Cuellar J, Perales-Calvo J, Muga A, Valpuesta JM, Moro F
J Biol Chem (2013) 288 pp. 15065-15074 [ DOI: doi:10.1074/jbc.M112.430595 Pubmed: 23580641 ]
- Shorter version of repe (repe 1-144) (32 kDa, Protein from Escherichia coli)
- Hsp40 (80 kDa, Protein from Escherichia coli)
- Dnaj:repe(1-144) complex (115 kDa, Sample)
Structural insights into the chaperone activity of Hsp40: DnaJ binds and remodels RepE
Cuellar J, Perales-Calvo J, Muga A, Valpuesta JM, Moro F
J Biol Chem (2013) 288 pp. 15065-15074 [ DOI: doi:10.1074/jbc.M112.430595 Pubmed: 23580641 ]
- Dnaj:repe54 complex (140 kDa, Sample)
- Replication initiator protein repe54 of plasmid mini-f (30 kDa, Protein from Escherichia coli)
- Hsp40 (80 kDa, Protein from Escherichia coli)
Pena A, Matilla I, Martin-Benito J, Valpuesta JM, Carrascosa JL, De la Cruz F, Cabezon E, Arechaga I
J Biol Chem (2012) 287 pp. 39925-39932 [ Pubmed: 23035111 DOI: doi:10.1074/jbc.M112.413849 ]
- Virb4 component of type iv transporter system (540 kDa, Protein from Escherichia coli)
- Hexameric trwk (540 kDa, Sample)
Electron Microscopy of THO complex
Pena A, Gewartowski K, Mroczek S, Cuellar J, Szykowska A, Prokop A, Czarnocki-Cieciura M, Piwowarski J, Tous C, Aguilera A, Carrascosa JL, Valpuesta JM, Dziembowski A
EMBO J (2012) 31 pp. 1605-1616 [ DOI: doi:10.1038/emboj.2012.10 Pubmed: 22314234 ]
- Tho2 (180 MDa, Protein from Saccharomyces cerevisiae)
- Tex1 (50 MDa, Protein from Saccharomyces cerevisiae)
- Yeast five-subunit tho complex (395 MDa, Sample)
- Mft1 (45 MDa, Protein from Saccharomyces cerevisiae)
- Hpr1 (90 MDa, Protein from Saccharomyces cerevisiae)
- Thp2 (30 MDa, Protein from Saccharomyces cerevisiae)
Resolution: 10.8 Å
EM Method: Single-particle
Fitted PDBs: 2xvr
Q-score: 0.09
Ionel A, Velazquez-Muriel JA, Luque D, Cuervo A, Caston JR, Valpuesta JM, Martin-Benito J, Carrascosa JL
J Biol Chem (2011) 286 pp. 234-242 [ DOI: doi:10.1074/jbc.M110.187211 Pubmed: 20962334 ]
Structure of the complex Nucleoplamsin:H2A-H2B histones.
Resolution: 19.5 Å
EM Method: Single-particle
Fitted PDBs: 2xql
Q-score: 0.071
Ramos I, Martin-Benito J, Finn R, Bretana L, Aloria K, Arizmendi JM, Ausio J, Muga A, Valpuesta JM, Prado A
J Biol Chem (2010) 285 pp. 33771-33778 [ Pubmed: 20696766 DOI: doi:10.1074/jbc.M110.150664 ]
- Nucleoplasmin-histone h2a-histone h2b complex (1-5-5). (270 kDa, Sample)
- Nucleoplasmin (110 kDa, Protein from Xenopus laevis)
- H2b histone (14 kDa, Protein from Gallus gallus)
- H2a histone (13 kDa, Protein from Gallus gallus)
Structure of the Nuclear Chaperone Nucleoplamsin.
Ramos I, Martin-Benito J, Finn R, Bretana L, Aloria K, Arizmendi JM, Ausio J, Muga A, Valpuesta JM, Prado A
J Biol Chem (2010) 285 pp. 33771-33778 [ DOI: doi:10.1074/jbc.M110.150664 Pubmed: 20696766 ]
- Nucleoplasmin chaperone (110 kDa, Sample)
- Nucleoplasmin (110 kDa, Protein from Xenopus laevis)