Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase

Chan, Michael K.; Mukund, Swarnalatha; Kletzin, Arnulf; Adams, Michael W. W.; Rees, Douglas C.

doi:10.1126/science.7878465

Cited by 575 publications

(509 citation statements)

References 62 publications

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“…From the various studies different featu,'es have been discussed as responsible for the increased conformational stability at all three levels of protein structure (c~,re region and secondary structure elements, interactions between domains and subunits): e.g. reduction of solvent acce~sible area and increase in the fraction of buried atoms [1], st~bilization of a-helices, strengthening of polypeptide chain teTmini and loops [2], shortening of loops [3], increase of ion bridges and hydrophobic interactions [4][5][6]. The observation that especially the subunit contacts are intensified by a strikin!…”

Section: Introductionmentioning

confidence: 99%

Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

1996

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Section: Introductionmentioning

confidence: 99%

Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

1996

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“…These include the overall amino acid composition (Argos et al, Menendez-Arias & Argos, 19891, site-specific amino acid replacement, such as proline in turns (Matthews et al, 1987; Watanabe et al, 1991), salt bridges (Perutz & Raidt, 1975), hydrogen bonding (Day et al, 1992;Tanner et al, 1996), hydrophobic interactions and packing (Yamada et al, 1990;Chan et al, 1995;Spassov et al, 1995). electrostatic interactions (Spassov et al, 1995), increased helix stability (Davies et al, 1993;Russell et al, 1994;Hennig et al, 1995), or disulfide bonds and metals (Fromme1 & Sander, 1989).…”

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confidence: 99%

Dynamics and unfolding pathways of a hyperthermophilic and a mesophilic rubredoxin

1997

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Molecular dynamics simulations in solution are performed for a rubredoxin from the hyperthermophilic archaeon Pymcoccus furiosus (RdPf) and one from the mesophilic organism Desulfovibrio vulgaris (RdDv). The two proteins are simulated at four temperatures: 300 K, 373 K, 473 K (two sets), and 500 K; the various simulations extended from 200 ps to 1,020 ps. At room temperature, the two proteins are stable, remain close to the crystal structure, and exhibit similar dynamic behavior; the RMS residue fluctuations are slightly smaller in the hyperthermophilic protein. An analysis of the average energy contributions in the two proteins is made; the results suggest that the intraprotein energy stabilizes RdPf relative to RdDv. At 373 K, the mesophilic protein unfolds rapidly (it begins to unfold at 300 ps), whereas the hyperthermophilic does not unfold over the simulation of 600 ps. This is in accord with the expected stability of the two proteins. At 473 K, where both proteins are expected to be unstable, unfolding behavior is observed within 200 ps and the mesophilic protein unfolds faster than the hyperthermophilic one. At 500 K, both proteins unfold; the hyperthermophilic protein does so faster than the mesophilic protein. The unfolding behavior for the two proteins is found to be very similar. Although the exact order of events differs from one trajectory to another, both proteins unfold first by opening of the loop region to expose the hydrophobic core. This is followed by unzipping of the @-sheet. The results obtained in the simulation are discussed in terms of the factors involved in flexibility and thermostability.

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“…3, Table 3). 6 ]glucose. The recombinant strain Z and a cis-configuration of the 4′ β and 3′ protons.…”

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confidence: 99%

Rearrangement reactions in the biosynthesis of molybdopterin

Rieder

Eisenreich

O’Brien

et al. 1998

European Journal of Biochemistry

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The genes moaABC of Escherichia coli were ligated into the expression vector pNCO113. The resulting plasmid was transformed into a moeA mutant of E. coli. From cultures of the recombinant strain, a pteridine designated compound Z could be isolated at 5 mg/liter. Compound Z is a product of precursor Z, a biosynthetic precursor of molybdopterin. Cultures of the recombinant E. coli strain were supplied with [U-13 C 6 ]glucose, [U-13 C 5 ]ribulose 5-phosphate, or [7-15 N,8-13 C]guanine. The culture medium also contained a large excess of unlabeled glucose. Compound Z as well as nucleosides obtained by hydrolysis of RNA were isolated from the bacterial cultures, and their heavy isotope distribution was investigated by one-dimensional and two-dimensional NMR spectroscopy. The labelling patterns of compound Z show that the carbon atoms of a pentose or pentulose are diverted to the ring atoms C6 and C7 and to the side chain atoms C2′, C3′ and C4′ of compound Z. Carbon atom C1′ of compound Z is derived from carbon atom C8 of a guanine derivative. The remodeling of the carbon skeleton of the pentose and purine moieties proceed via intramolecular rearrangement reactions.Keywords : biosynthesis of molybdopterin; NMR; rearrangement reaction ; Escherichia coli. Fig. 1) is a nonconjugated tetrahy-acts as cofactor of xanthine dehydrogenase and sulphite oxidase, among others [7]. Genetic defects of the molybdopterin pathway dropterin derivative complexed to a molybdenum ion and serves as cofactor for a variety of enzyme-catalysed redox reactions are conducive to severe neurological deficiencies in man (for review see [14]

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Structure of a Hyperthermophilic Tungstopterin Enzyme, Aldehyde Ferredoxin Oxidoreductase

Cited by 575 publications

References 62 publications

Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

Tetrameric triosephosphate isomerase from hyperthermophilic Archaea

Dynamics and unfolding pathways of a hyperthermophilic and a mesophilic rubredoxin

Rearrangement reactions in the biosynthesis of molybdopterin

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