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Structure and function of archaeal prefoldin, a co-chaperone of group II chaperonin.
Ohtaki A, Noguchi K, Yohda M. Ohtaki A, et al. Front Biosci (Landmark Ed). 2010 Jan 1;15:708-17. doi: 10.2741/3641. Front Biosci (Landmark Ed). 2010. PMID: 20036841 Review.
Prefoldin is a chaperone that acts as a co-factor of group II chaperonins in eukaryotes and archaea. It assists proper folding of protein by capturing nonnative proteins and delivering it to the group II chaperonin. Eukaryotic prefoldin is a multiple subunit …
Prefoldin is a chaperone that acts as a co-factor of group II chaperonins in eukaryotes and archaea. It assists proper folding …
Properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus HB8.
Igari S, Ohtaki A, Yamanaka Y, Sato Y, Yohda M, Odaka M, Noguchi K, Yamada K. Igari S, et al. PLoS One. 2011;6(8):e23716. doi: 10.1371/journal.pone.0023716. Epub 2011 Aug 15. PLoS One. 2011. PMID: 21858212 Free PMC article.
METHODOLOGY/PRINCIPAL FINDINGS: MTHFR from Thermus thermophilus HB8, a homologue of Escherichia coli MetF, has been expressed in E. coli and purified. ...Free FAD could be incorporated into the apo-subunit of the purified Thermus enzyme after purification, forming a
METHODOLOGY/PRINCIPAL FINDINGS: MTHFR from Thermus thermophilus HB8, a homologue of Escherichia coli MetF, has been expressed in E. c …
Thermodynamic characterization of the interaction between prefoldin and group II chaperonin.
Sahlan M, Zako T, Tai PT, Ohtaki A, Noguchi K, Maeda M, Miyatake H, Dohmae N, Yohda M. Sahlan M, et al. J Mol Biol. 2010 Jun 18;399(4):628-36. doi: 10.1016/j.jmb.2010.04.046. Epub 2010 Apr 29. J Mol Biol. 2010. PMID: 20434454
Prefoldin (PFD) is a hexameric chaperone that captures a protein substrate and transfers it to a group II chaperonin (CPN) to complete protein folding. We have studied the interaction between PFD and CPN using those from a hyperthermophilic archaeon, T …
Prefoldin (PFD) is a hexameric chaperone that captures a protein substrate and transfers it to a group II chaperonin (C …
Crystal structure of 1-deoxy-d-xylulose 5-phosphate reductoisomerase from the hyperthermophile Thermotoga maritima for insights into the coordination of conformational changes and an inhibitor binding.
Takenoya M, Ohtaki A, Noguchi K, Endo K, Sasaki Y, Ohsawa K, Yajima S, Yohda M. Takenoya M, et al. J Struct Biol. 2010 Jun;170(3):532-9. doi: 10.1016/j.jsb.2010.03.015. Epub 2010 Mar 29. J Struct Biol. 2010. PMID: 20353826
The structure without fosmidomycin but unexpectedly bound with 2-methyl-2,4-pentanediol (MPD), revealing a new extra space available for potential drug design. This structure adopted the closed form by rigid domain rotation but without the flexible loop over the active sit …
The structure without fosmidomycin but unexpectedly bound with 2-methyl-2,4-pentanediol (MPD), revealing a new extra space available …
Crystal structures of the lumazine protein from Photobacterium kishitanii in complexes with the authentic chromophore, 6,7-dimethyl- 8-(1'-D-ribityl) lumazine, and its analogues, riboflavin and flavin mononucleotide, at high resolution.
Sato Y, Shimizu S, Ohtaki A, Noguchi K, Miyatake H, Dohmae N, Sasaki S, Odaka M, Yohda M. Sato Y, et al. J Bacteriol. 2010 Jan;192(1):127-33. doi: 10.1128/JB.01015-09. J Bacteriol. 2010. PMID: 19854891 Free PMC article.
Lumazine protein (LumP) is a fluorescent accessory protein having 6,7-dimethyl-8-(1'-d-ribityl) lumazine (DMRL) as its authentic chromophore. ...In LumP-DMRL, the side chain of Gln65 is close to the ring system, and a new water molecule that stabilizes the ligand is …
Lumazine protein (LumP) is a fluorescent accessory protein having 6,7-dimethyl-8-(1'-d-ribityl) lumazine (DMRL) as its authentic chro …
Structure and molecular dynamics simulation of archaeal prefoldin: the molecular mechanism for binding and recognition of nonnative substrate proteins.
Ohtaki A, Kida H, Miyata Y, Ide N, Yonezawa A, Arakawa T, Iizuka R, Noguchi K, Kita A, Odaka M, Miki K, Yohda M. Ohtaki A, et al. J Mol Biol. 2008 Feb 29;376(4):1130-41. doi: 10.1016/j.jmb.2007.12.010. Epub 2007 Dec 8. J Mol Biol. 2008. PMID: 18201719
Prefoldin (PFD) is a heterohexameric molecular chaperone complex in the eukaryotic cytosol and archaea with a jellyfish-like structure containing six long coiled-coil tentacles. ...PhPFD has a jellyfish-like structure with six long coiled-coil tentacles and …
Prefoldin (PFD) is a heterohexameric molecular chaperone complex in the eukaryotic cytosol and archaea with a jellyfish-like s …
Structure of aspartate racemase complexed with a dual substrate analogue, citric acid, and implications for the reaction mechanism.
Ohtaki A, Nakano Y, Iizuka R, Arakawa T, Yamada K, Odaka M, Yohda M. Ohtaki A, et al. Proteins. 2008 Mar;70(4):1167-74. doi: 10.1002/prot.21528. Proteins. 2008. PMID: 17847084
In this study, we have determined the crystal structure of an inactive mutant PhAspR complexed with a citric acid (Cit) at a resolution of 2.0 A. ...The distance between the thiolates was estimated to be 7.4 A, representing a catalytic state and …
In this study, we have determined the crystal structure of an inactive mutant PhAspR complexed with a citric acid (Cit) at a r …
Structure of a complex of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with maltohexaose demonstrates the important role of aromatic residues at the reducing end of the substrate binding cleft.
Ohtaki A, Mizuno M, Yoshida H, Tonozuka T, Sakano Y, Kamitori S. Ohtaki A, et al. Carbohydr Res. 2006 Jun 12;341(8):1041-6. doi: 10.1016/j.carres.2006.01.029. Epub 2006 Mar 27. Carbohydr Res. 2006. PMID: 16564038
The crystal structure of an inactive mutant TVAII in a complex with maltohexaose was determined at a resolution of 2.1A. TVAII adopts a dimeric structure to form two catalytic sites, where substrates are found to bind. ...Trp356 drastically changes its side-c …
The crystal structure of an inactive mutant TVAII in a complex with maltohexaose was determined at a resolution of 2.1A. TVAII …
Structure and direct electrochemistry of cytochrome P450 from the thermoacidophilic crenarchaeon, Sulfolobus tokodaii strain 7.
Oku Y, Ohtaki A, Kamitori S, Nakamura N, Yohda M, Ohno H, Kawarabayasi Y. Oku Y, et al. J Inorg Biochem. 2004 Jul;98(7):1194-9. doi: 10.1016/j.jinorgbio.2004.05.002. J Inorg Biochem. 2004. PMID: 15219985
P450st was crystallized in an orthorhombic system with the space group P2(1)2(1)2(1) and cell dimensions of a=53.6 A, b=55.1 A, and c=130.9 A, and the structure was determined at a 3.0 A resolution. ...Direct electrochemistry of P450st in …
P450st was crystallized in an orthorhombic system with the space group P2(1)2(1)2(1) and cell dimensions of a=53.6 A, b=55.1 …
The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
Mizuno M, Tonozuka T, Uechi A, Ohtaki A, Ichikawa K, Kamitori S, Nishikawa A, Sakano Y. Mizuno M, et al. Eur J Biochem. 2004 Jun;271(12):2530-8. doi: 10.1111/j.1432-1033.2004.04183.x. Eur J Biochem. 2004. PMID: 15182368
We then determined the crystal structure of TVA II complexed with 4(2)-alpha-panosylpanose (4(2)-P2), which was produced by transglycosylation from 4(3)-P2, at 2.2-A resolution. The shape of the active cleft of TVA II is unique among those of alpha-amylase family enzymes d …
We then determined the crystal structure of TVA II complexed with 4(2)-alpha-panosylpanose (4(2)-P2), which was produced by transglycosylati …
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