All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly.
about
Structural and functional analysis of phytotoxin toxoflavin-degrading enzymeMicrobial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamilyAccommodation of a highly symmetric core within a symmetric protein superfoldCatalytic Mechanism of Bleomycin N-Acetyltransferase Proposed on the Basis of Its Crystal StructureToxoflavin Lyase Requires a Novel 1-His-2-Carboxylate Facial Triad,Atomic resolution structure of EhpR: phenazine resistance in Enterobacter agglomerans Eh1087 follows principles of bleomycin/mitomycin C resistance in other bacteriaC-terminal β-strand swapping in a consensus-derived fibronectin Type III scaffoldMolecular basis for the stabilization and inhibition of 2, 3-dihydroxybiphenyl 1,2-dioxygenase by t-butanolGlyoxalase I of the malarial parasite Plasmodium falciparum: evidence for subunit fusionSystematic detection of internal symmetry in proteins using CE-SymmThree-dimensional domain swapping in the protein structure space.Expression of Xhdsi-1VOC, a novel member of the vicinal oxygen chelate (VOC) metalloenzyme superfamily, is up-regulated in leaves and roots during desiccation in the resurrection plant Xerophyta humilis (Bak) Dur and SchinzCharacteristic Variations and Similarities in Biochemical, Molecular, and Functional Properties of Glyoxalases across Prokaryotes and Eukaryotes.Whole-Genome Identification and Expression Pattern of the Vicinal Oxygen Chelate Family in Rapeseed (Brassica napus L.).Alternative epimerization in C(7)N-aminocyclitol biosynthesis is catalyzed by ValD, a large protein of the vicinal oxygen chelate superfamily.Biosynthetic gene cluster of cetoniacytone A, an unusual aminocyclitol from the endosymbiotic Bacterium Actinomyces sp. Lu 9419.Structural variation in bacterial glyoxalase I enzymes: investigation of the metalloenzyme glyoxalase I from Clostridium acetobutylicum.Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases.Protein acrobatics in pairs--dimerization via domain swapping.Metal-Directed Design of Supramolecular Protein Assemblies.1.6 A crystal structure of a PA2721 protein from pseudomonas aeruginosa--a potential drug-resistance protein.Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.Glyoxalase biochemistry.Distinct classes of glyoxalase I: metal specificity of the Yersinia pestis, Pseudomonas aeruginosa and Neisseria meningitidis enzymes.Intersubunit interaction and catalytic activity of catechol 2,3-dioxygenases.Investigation of metal binding and activation of Escherichia coli glyoxalase I: kinetic, thermodynamic and mutagenesis studies.Characterization of a novel thermostable Mn(II)-dependent 2,3-dihydroxybiphenyl 1,2-dioxygenase from a polychlorinated biphenyl- and naphthalene-degrading Bacillus sp. JF8.Modeling and analysis of the structure of the thermostable catechol 2,3-dioxygenase from Bacillus Stearothermophilus.
P2860
Q21135296-DC9EA348-DC62-4961-8DD6-6199F4B43849Q24548519-73A79063-CBE7-47AA-BF9C-F928F0F4D322Q27642593-3F6DEFCB-C8A0-4EE2-B81B-9A0FFA563DF1Q27658060-CC65A5BF-B73A-4A83-9F0E-8413439B0B65Q27666327-685F08D3-9D1A-4086-B8FC-1D41276E441AQ27671812-C3F2B097-BECE-494D-9EE3-9A685C5509CFQ27688045-DDA677AC-2AA7-4AA7-A717-9CF7508364C4Q27766353-F96F54D3-F025-4918-BCBE-7FD3D545A976Q27973444-7F37BBB4-8669-4212-B5BC-90CD35CEC74CQ28645866-898C7A90-B30E-412D-9D86-3AB659C5EC0AQ30414200-0C42FC42-DA30-41F0-8E7B-F9B673F9952CQ33369396-27145508-22FC-4D59-937F-B00CBF46D5E3Q33624183-8B699EBF-065C-47E4-B4B1-0F76BF937B3DQ33650338-C8EEEC5D-18DA-452A-8FD7-1A1FE58BEC4FQ34983554-DD740D35-AF9A-40A9-91EA-2FBF423466DAQ35105705-420A5CFA-1D52-4277-B07B-C85B175A5525Q35516038-95CCF491-C8F2-4D85-BB63-B2C5AB34AD46Q37096285-C7DC6A42-55BE-4745-BE33-F396004CBF39Q37177524-96904318-3BEA-4267-8914-8BFC9E00AA91Q37461387-C95018DD-9FFD-4467-A4DC-F79339609A5BQ37471224-F3F7DF89-EB22-47F2-86BA-272CF7DCBF4BQ37860600-D03A9160-EA71-4828-9174-1D23B8282FF1Q38629015-E979BACE-D5BD-4C80-801E-F17502F1E973Q41461864-B3A3DEAB-8EBD-4DC6-8E98-71D86372AE90Q42157317-0F711194-190D-4A80-B546-D73C23EA8979Q42242378-AE930AD7-5390-4A74-990D-EA622929869DQ43032877-4EC81BA7-ACED-49A1-B7FD-EFE1691421EDQ43743824-4EB86D5A-0FE5-47D4-87A6-EFE2F3295F27
P2860
All in the family: structural and evolutionary relationships among three modular proteins with diverse functions and variable assembly.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
All in the family: structural ...... nctions and variable assembly.
@ast
All in the family: structural ...... nctions and variable assembly.
@en
type
label
All in the family: structural ...... nctions and variable assembly.
@ast
All in the family: structural ...... nctions and variable assembly.
@en
prefLabel
All in the family: structural ...... nctions and variable assembly.
@ast
All in the family: structural ...... nctions and variable assembly.
@en
P2093
P2860
P356
P1433
P1476
All in the family: structural ...... nctions and variable assembly.
@en
P2093
P2860
P304
P356
10.1002/PRO.5560070801
P577
1998-08-01T00:00:00Z