Crystallization and preliminary X-ray analyses of desulfurization enzyme DszB and its C27S mutant complexed with biphenyl-2-sulfinic acid
DszB is a hydrolase involved in the biodegradation of dibenzothiophene in the soil bacterium Rhodococcus sp. IGTS8. DszB catalyzes the hydrolysis of 2′‐hydroxybiphenyl‐2‐sulfinic acid to sulfite and biphenyl‐2‐ol. DszB and DszB C27S mutant complexed with biphenyl‐2‐sulfinic acid were crystallized an...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-09, Vol.60 (9), p.1636-1638 |
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Sprache: | eng |
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Zusammenfassung: | DszB is a hydrolase involved in the biodegradation of dibenzothiophene in the soil bacterium Rhodococcus sp. IGTS8. DszB catalyzes the hydrolysis of 2′‐hydroxybiphenyl‐2‐sulfinic acid to sulfite and biphenyl‐2‐ol. DszB and DszB C27S mutant complexed with biphenyl‐2‐sulfinic acid were crystallized and preliminary X‐ray crystallographic analyses were conducted. The crystals of DszB were found to belong to the orthorhombic P212121 space group, with unit‐cell parameters a = 36.7, b = 82.6, c = 139.6 Å, and to contain one molecule of DszB in the asymmetric unit. Crystals of DszB C27S complexed with biphenyl‐2‐sulfinic acid belong to space group C2, with unit‐cell parameters a = 153.4, b = 45.9, c = 112.9 Å, β = 115.93°. The calculated Matthews coefficient VM for the C2 crystals is approximately 2.3 Å3 Da−1 if two molecules of DszB are present in the asymmetric unit. |
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ISSN: | 1399-0047 0907-4449 1399-0047 |
DOI: | 10.1107/S0907444904017627 |