Crystal Structure of Dimethyl Sulfoxide Reductase fromRhodobacter capsulatusat 1.88 Å Resolution

Schneider, Frank; Löwe, Jan; Huber, Robert; Schindelin, Hermann; Kisker, Caroline; Knäblein, Jörg

doi:10.1006/jmbi.1996.0555

Cited by 261 publications

(232 citation statements)

References 48 publications

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“…Owing to this property, the octahedral cluster ion Ta 6 Br 2 12 has been introduced as a powerful derivatization reagent for phasing macromolecular crystal structures (Schneider & Lindqvist, 1994;Kna È blein et al, 1997). So far, it has been mostly used for phasing large crystal structures of proteins and complexes at low resolution (Lindvist et al, 1992;Schneider et al, 1996;Thygesen et al, 1996;Ban et al, 2000;Gomis-Ru È th & Coll, 2001). Indeed, at resolutions lower than 5 A Ê the cluster scatters as a super-atom, which enhances its isomorphous and anomalous diffraction signals.…”

Section: Introductionmentioning

confidence: 99%

Phasing at high resolution using Ta₆Br₁₂cluster

Sankaran

Dauter

2003

Acta Crystallogr D Biol Cryst

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The Ta 6 Br 2 12 cluster compound is known to be a powerful reagent for derivatization of crystals of large macromolecules at low resolution. The cluster is a regular octahedron of six Ta atoms with 12 bridging Br atoms at the edges of the octahedron. The cluster is compact, of approximately spherical shape, with a radius of about 6 A Ê . Both tantalum and bromine display a signi®cant anomalous diffraction signal at their absorption edges at 1.25 and 0.92 A Ê , respectively. At resolutions lower than 5 A Ê the tantalum cluster behaves as a super-atom and provides very large isomorphous and anomalous signals, which signi®cantly diminish at about 4 A Ê . However, beyond 3 A Ê the individual Ta atoms can be resolved and the phasing power of the cluster increases again. The Ta 6 Br 2 12 cluster has been used for phasing four different proteins at high resolution. Ta 6 Br 2 12 appeared to be a mild derivatization reagent and, despite partial incorporation, led to a successful solution of crystal structures by the singlewavelength anomalous diffraction (SAD) approach.

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Section: Introductionmentioning

confidence: 99%

Phasing at high resolution using Ta₆Br₁₂cluster

Sankaran

Dauter

2003

Acta Crystallogr D Biol Cryst

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“…The first crystal structure reported for a member of this family was DMSO reductase [15,16]. However, our knowledge about this family was greatly increased with the study of nitrate reductase, which catalyzes the reduction of nitrate to nitrite, and formate dehydrogenase, involved in the oxidation of formate to carbon dioxide.…”

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confidence: 99%

Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases

et al. 2004

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Molybdenum and tungsten are second-and third-row transition elements, respectively, which are found in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen atom transfer reactions. Mononuclear Mo-containing enzymes have been classified into three families: xanthine oxidase, DMSO reductase, and sulfite oxidase. The proteins of the DMSO reductase family present the widest diversity of properties among its members and our knowledge about this family was greatly broadened by the study of the enzymes nitrate reductase and formate dehydrogenase, obtained from different sources. We discuss in this review the information of the better characterized examples of these two types of Mo enzymes and W enzymes closely related to the members of the DMSO reductase family. We briefly summarize, also, the few cases reported so far for enzymes that can function either with Mo or W at their active site.

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“…The first crystal structure for a protein of this family was the one reported for DMSOR from Rhodobacter sphaeroides (6). Members of the DMSOR family share the Mo-containing ␣-subunit, such as DMSOR (6)(7)(8), formate dehydrogenase (FDH)-H (9), and dissimilatory nitrate reductase (NIR) (10), but may also have one or two additional small subunits as observed in arsenite oxidase (11) and in tungsten-containing FDH-T (12) (␣-and ␤-subunits), and in NIR A (NARGHI) (13) and FDH-N (14) (␣-, ␤-, and ␥-subunits). The only protein ligand to the Mo ion is either a Ser (DMSOR, TH), Cys (dissimilatory NIR), Asp (NIR A), or seleno-Cys (FDHs).…”

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confidence: 99%

Crystal structure of pyrogallol–phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols

Messerschmidt

Niessen

Abt

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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The Mo enzyme transhydroxylase from the anaerobic microorganism Pelobacter acidigallici catalyzes the conversion of pyrogallol to phloroglucinol. Such trihydroxybenzenes and their derivatives represent important building blocks of plant polymers. None of the transferred hydroxyl groups originates from water during transhydroxylation; instead a cosubstrate, such as 1,2,3,5-tetrahydroxybenzene, is used in a reaction without apparent electron transfer. Here, we report on the crystal structure of the enzyme in the reduced Mo(IV) state, which we solved by single anomalousdiffraction technique. It represents the largest structure (1,149 amino acid residues per molecule, 12 independent molecules per unit cell), which has been solved so far by single anomalousdiffraction technique. Tranhydroxylase is a heterodimer, with the active Mo-molybdopterin guanine dinucleotide (MGD)2 site in the ␣-subunit, and three [4FeO4S] centers in the ␤-subunit. The latter subunit carries a seven-stranded, mainly antiparallel ␤-barrel domain. We propose a scheme for the transhydroxylation reaction based on 3D structures of complexes of the enzyme with various polyphenols serving either as substrate or inhibitor.

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Crystal Structure of Dimethyl Sulfoxide Reductase fromRhodobacter capsulatusat 1.88 Å Resolution

Cited by 261 publications

References 48 publications

Phasing at high resolution using Ta₆Br₁₂cluster

Phasing at high resolution using Ta₆Br₁₂cluster

Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases

Crystal structure of pyrogallol–phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols

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Crystal Structure of Dimethyl Sulfoxide Reductase fromRhodobacter capsulatusat 1.88 Å Resolution

Cited by 261 publications

References 48 publications

Phasing at high resolution using Ta6Br12cluster

Phasing at high resolution using Ta6Br12cluster

Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases

Crystal structure of pyrogallol–phloroglucinol transhydroxylase, an Mo enzyme capable of intermolecular hydroxyl transfer between phenols

Contact Info

Product

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Phasing at high resolution using Ta₆Br₁₂cluster

Phasing at high resolution using Ta₆Br₁₂cluster