The solution structure of the 60-residue 1[Fe4-S4] ferredoxin from the hyperthermophilic bacterium Thermotoga maritima was determined based on 683 distance and 35 dihedral angle restraints that were obtained from NMR data. In addition, data known from crystallographic studies of ferredoxins was used for modeling of the iron-sulfur cluster and its environment. The protein shows a globular fold very similar to the fold of the related 1[Fe4-S4] ferredoxins from Desulfovibrio gigas and Desulfovibrio africanus, and elements of regular secondary structure similar to those in other ferredoxins were found in the T. maritima protein. In particular, the T. maritima protein displayed a beta-sheet structure made up of strands located at the very NH(2) and COOH termini of the protein, and an internal alpha-helix. The internal beta-sheet observed in the D. gigas and D. africanus ferredoxins could not be confirmed in T. maritima ferredoxin and is thus suggested to be only weakly present or even absent in this protein. This result suggests that thermostability in ferredoxins is not necessarily correlated with the content of stable elements of regular secondary structure.
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima
Abstract The bacterial histidine autokinase CheA contains a histidine phosphotransfer (Hpt) domain that accepts a phosphate from the catalytic domain and donates the phosphate to either target response regulator protein, CheY or CheB. The Hpt domain forms a helix-bundle structure with a conserved four-helix bundle motif and a variable fifth helix. Observation of two nearly equally populated conformations in the crystal...
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[NMR paper] NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins.
NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins.
Related Articles NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins.
Protein Sci. 2005 Nov;14(11):2880-6
Authors: Almeida MS, Herrmann T, Peti W, Wilson IA, Wüthrich K
The NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima represents an alpha/beta-topology formed by the regular secondary structures...
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[NMR paper] NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima.
NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima.
Related Articles NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima.
Proteins. 2005 Aug 15;60(3):552-7
Authors: Columbus L, Peti W, Etezady-Esfarjani T, Herrmann T, Wüthrich K
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[NMR paper] NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima.
NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima.
Related Articles NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima.
Proteins. 2005 May 1;59(2):387-90
Authors: Peti W, Herrmann T, Zagnitko O, Grzechnik SK, Wüthrich K
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11-25-2010 08:21 PM
[NMR paper] NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprot
NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure.
Related Articles NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure.
J Struct Funct Genomics. 2005;6(1):51-62
Authors: Penhoat CH, Li Z, Atreya HS, Kim S, Yee A, Xiao R, Murray D, Arrowsmith CH, Szyperski T
The 150-residue protein TM1509 is encoded in gene YF09_THEMA of Thermotoga maritima. TM1509 has so far no functional annotation and belongs to protein family...
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11-24-2010 11:14 PM
[NMR paper] NMR for structural proteomics of Thermotoga maritima: screening and structure determi
NMR for structural proteomics of Thermotoga maritima: screening and structure determination.
Related Articles NMR for structural proteomics of Thermotoga maritima: screening and structure determination.
J Struct Funct Genomics. 2004;5(3):205-15
Authors: Peti W, Etezady-Esfarjani T, Herrmann T, Klock HE, Lesley SA, Wüthrich K
This paper describes the NMR screening of 141 small (
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[NMR paper] An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-
An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas.
Related Articles An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas.
Biochemistry. 1994 May 31;33(21):6424-32
Authors: Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA
A model for the solution structure of oxidized putidaredoxin (Pdx), a 106-residue globular protein containing a Fe2S2 cluster, has been determined using homonuclear NMR methods. Pdx is the first of the...
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[NMR paper] An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-
An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas.
Related Articles An NMR-derived model for the solution structure of oxidized putidaredoxin, a 2-Fe, 2-S ferredoxin from Pseudomonas.
Biochemistry. 1994 May 31;33(21):6424-32
Authors: Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA
A model for the solution structure of oxidized putidaredoxin (Pdx), a 106-residue globular protein containing a Fe2S2 cluster, has been determined using homonuclear NMR methods. Pdx is the first of the...