Deciphering the zinc coordination properties of the prokaryotic zinc finger domain: The solution structure characterization of Ros87 H42A functional mutant (511 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2014 Feb; 131: 30-36.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.444, 5-year impact factor: 3.447
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84887596747&partnerID=40&md5=5461f40d5cfa912e1557bfd35bd4526c
Keywords: H D Exchange, Metal Binding Proteins, Prokaryotic Zinc Finger, Amino Acid Derivative, Histidine Derivative, Reactive Oxygen Metabolite, Alpha Helix, Article, Binding Affinity, Controlled Study, Dna Binding, Isothermal Titration Calorimetry, Nuclear Magnetic Resonance, Spectrophotometry, Zinc Finger Motif, Eukaryota, Agrobacterium Tumefaciens, Bacterial Proteins, Binding Sites, Deuterium, Hydrogen, Models, Molecular, Biomolecular, Protein Conformation, Protein Folding, Protein Structure, Tertiary, Agrobacterium Tumefaciens Chemistry, Bacterial Proteins Chemistry Genetics Metabolism, Dna Metabolism, Deuterium Chemistry, Hydrogen Chemistry, Zinc Chemistry Metabolism, Zinc Fingers Genetics,
Affiliations:
*** IBB - CNR ***
Department of Environmental, Biological and Pharmaceutical Sciences and Technology, Via Vivaldi 43, 81100 Caserta, Italy
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy
Interuniversity Centre for Research on Bioactive Peptides (CIRPEB), University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy
References:
Not available.
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2014 Feb; 131: 30-36.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 3.444, 5-year impact factor: 3.447
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84887596747&partnerID=40&md5=5461f40d5cfa912e1557bfd35bd4526c
Keywords: H D Exchange, Metal Binding Proteins, Prokaryotic Zinc Finger, Amino Acid Derivative, Histidine Derivative, Reactive Oxygen Metabolite, Alpha Helix, Article, Binding Affinity, Controlled Study, Dna Binding, Isothermal Titration Calorimetry, Nuclear Magnetic Resonance, Spectrophotometry, Zinc Finger Motif, Eukaryota, Agrobacterium Tumefaciens, Bacterial Proteins, Binding Sites, Deuterium, Hydrogen, Models, Molecular, Biomolecular, Protein Conformation, Protein Folding, Protein Structure, Tertiary, Agrobacterium Tumefaciens Chemistry, Bacterial Proteins Chemistry Genetics Metabolism, Dna Metabolism, Deuterium Chemistry, Hydrogen Chemistry, Zinc Chemistry Metabolism, Zinc Fingers Genetics,
Affiliations:
*** IBB - CNR ***
Department of Environmental, Biological and Pharmaceutical Sciences and Technology, Via Vivaldi 43, 81100 Caserta, Italy
Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, 80134 Naples, Italy
Interuniversity Centre for Research on Bioactive Peptides (CIRPEB), University of Naples Federico II, Via Mezzocannone 16, 80134 Naples, Italy
References:
Not available.
Deciphering the zinc coordination properties of the prokaryotic zinc finger domain: The solution structure characterization of Ros87 H42A functional mutant
The zinc coordination sphere in prokaryotic zinc finger domain is extremely versatile and influences the stability and the folding property of the domain. Of a particular interest is the fourth zinc coordinating position, which is frequently occupied by two successive histidines, both able to coordinate the metal ion. To clarify their structural and functional role we report the NMR solution structure and the dynamics behavior of Ros87 H42A, which is a functional mutant of Ros87, the DNA binding domain of the Ros protein containing a prokaryotic Cys(2)His(2) zinc finger domain. The structural analysis indicates that reducing the spacer among the two coordinating histidines from 4 (among His37 and His42) amino acids to 3 (among His37 and His41) increases the helicity of the first a-helix. At the same time, the second helix appears more mobile in the mu s-ms timescale and the hydrophobic core is reduced. These data explain the high frequency of three-residue His spacers in the eukaryotic zinc finger domain and their absence in the prokaryotic counterpart. Furthermore, the structural comparison shows that the second coordination position is more sensitive to H42A mutation with respect to the first and the third position, providing the rationale of the high variability of the second and the fourth zinc coordinating position in Ros homologs, which adopt different metal coordination but preserve similar tertiary structures and DNA binding activities. Finally, H/D exchange measurements and NMR thermal unfolding analysis indicate that this mutant likely unfolds via a different mechanism with respect to the wild-type. (C) 2013 Published by Elsevier Inc.
The zinc coordination sphere in prokaryotic zinc finger domain is extremely versatile and influences the stability and the folding property of the domain. Of a particular interest is the fourth zinc coordinating position, which is frequently occupied by two successive histidines, both able to coordinate the metal ion. To clarify their structural and functional role we report the NMR solution structure and the dynamics behavior of Ros87 H42A, which is a functional mutant of Ros87, the DNA binding domain of the Ros protein containing a prokaryotic Cys(2)His(2) zinc finger domain. The structural analysis indicates that reducing the spacer among the two coordinating histidines from 4 (among His37 and His42) amino acids to 3 (among His37 and His41) increases the helicity of the first a-helix. At the same time, the second helix appears more mobile in the mu s-ms timescale and the hydrophobic core is reduced. These data explain the high frequency of three-residue His spacers in the eukaryotic zinc finger domain and their absence in the prokaryotic counterpart. Furthermore, the structural comparison shows that the second coordination position is more sensitive to H42A mutation with respect to the first and the third position, providing the rationale of the high variability of the second and the fourth zinc coordinating position in Ros homologs, which adopt different metal coordination but preserve similar tertiary structures and DNA binding activities. Finally, H/D exchange measurements and NMR thermal unfolding analysis indicate that this mutant likely unfolds via a different mechanism with respect to the wild-type. (C) 2013 Published by Elsevier Inc.
Deciphering the zinc coordination properties of the prokaryotic zinc finger domain: The solution structure characterization of Ros87 H42A functional mutant
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Deciphering the zinc coordination properties of the prokaryotic zinc finger domain: The solution structure characterization of Ros87 H42A functional mutant
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View Export to BibTeX Export to EndNote
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Impact Factor: 2.733
View Export to BibTeX Export to EndNote
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Impact Factor: 2.425
View Export to BibTeX Export to EndNote
19 Records (19 excluding Abstracts).
Total impact factor: 65.42 (65.42 excluding Abstracts).
Total 5 year impact factor: 63.967 (63.967 excluding Abstracts).
Total impact factor: 65.42 (65.42 excluding Abstracts).
Total 5 year impact factor: 63.967 (63.967 excluding Abstracts).
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