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Hybrid cluster proteins (HCPs) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at 1.25 A resolution using synchrotron radiation.

Macedo S, Mitchell EP, Romão CV, Cooper SJ, Coelho R, Liu MY, Xavier AV, LeGall J, Bailey S, Garner DC, Hagen WR, Teixeira M, Carrondo MA, Lindley P
J Biol Inorg Chem 7 514-25 (2002)
Related entries: 1gn9, 1gnt

Cited: 13 times
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Abstract

The structures of the hybrid cluster proteins (HCPs) from the sulfate-reducing bacteria Desulfovibrio desulfuricans (ATCC 27774) and Desulfovibrio vulgaris (Hildenborough) have been elucidated at a resolution of 1.25 A using X-ray synchrotron radiation techniques. In the case of the D. desulfuricans protein, protein isolation, purification, crystallization and X-ray data collection were carried out under strict anaerobic conditions, whereas for the D. vulgaris protein the conditions were aerobic. However, both structures are essentially the same, comprising three domains and two iron-sulfur centres. One of these centres situated near the exterior of the molecules in domain 1 is a cubane [4Fe-4S] cluster, whereas the other, located at the interface of the three domains, contains the unusual four-iron cluster initially found in the D. vulgaris protein. Details of the structures and the associated EPR spectroscopy of the D. desulfuricans protein are reported herein. These structures show that the nature of the hybrid cluster, containing both oxygen and sulfur bridges, is independent of the presence of oxygen in the isolation and crystallization procedure and also does not vary significantly with changes in the oxidation state. The structures and amino acid sequences of the HCP are compared with the recently elucidated structure of the catalytic subunit of a carbon monoxide dehydrogenase from Carboxydothermus hydrogenoformans and related dehydrogenases. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00775-001-0326-y.

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  2. Structural and biochemical elucidation of class I hybrid cluster protein natively extracted from a marine methanogenic archaeon. Lemaire ON, Belhamri M, Wagner T. Front Microbiol 14 1179204 (2023)


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  1. A Multiplex Enzymatic Machinery for Cellular Protein S-nitrosylation. Seth D, Hess DT, Hausladen A, Wang L, Wang YJ, Stamler JS. Mol Cell 69 451-464.e6 (2018)
  2. Xenon in and at the end of the tunnel of bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase. Doukov TI, Blasiak LC, Seravalli J, Ragsdale SW, Drennan CL. Biochemistry 47 3474-3483 (2008)
  3. X-ray crystallographic and EPR spectroscopic analysis of HydG, a maturase in [FeFe]-hydrogenase H-cluster assembly. Dinis P, Suess DL, Fox SJ, Harmer JE, Driesener RC, De La Paz L, Swartz JR, Essex JW, Britt RD, Roach PL. Proc Natl Acad Sci U S A 112 1362-1367 (2015)
  4. The role of the hybrid cluster protein in oxidative stress defense. Almeida CC, Romão CV, Lindley PF, Teixeira M, Saraiva LM. J Biol Chem 281 32445-32450 (2006)
  5. Hydroxylamine assimilation by Rhodobacter capsulatus E1F1. requirement of the hcp gene (hybrid cluster protein) located in the nitrate assimilation nas gene region for hydroxylamine reduction. Cabello P, Pino C, Olmo-Mira MF, Castillo F, Roldán MD, Moreno-Vivián C. J Biol Chem 279 45485-45494 (2004)
  6. Hybrid cluster proteins and flavodiiron proteins afford protection to Desulfovibrio vulgaris upon macrophage infection. Figueiredo MC, Lobo SA, Sousa SH, Pereira FP, Wall JD, Nobre LS, Saraiva LM. J Bacteriol 195 2684-2690 (2013)
  7. Reduced hybrid cluster proteins (HCP) from Desulfovibrio desulfuricans ATCC 27774 and Desulfovibrio vulgaris (Hildenborough): X-ray structures at high resolution using synchrotron radiation. Aragão D, Macedo S, Mitchell EP, Romão CV, Liu MY, Frazão C, Saraiva LM, Xavier AV, LeGall J, van Dongen WMAM, Hagen WR, Teixeira M, Carrondo MA, Lindley P. J Biol Inorg Chem 8 540-548 (2003)
  8. The mammalian DUF59 protein Fam96a forms two distinct types of domain-swapped dimer. Chen KE, Richards AA, Ariffin JK, Ross IL, Sweet MJ, Kellie S, Kobe B, Martin JL. Acta Crystallogr D Biol Crystallogr 68 637-648 (2012)
  9. A Morphing [4Fe-3S-nO]-Cluster within a Carbon Monoxide Dehydrogenase Scaffold. Jeoung JH, Fesseler J, Domnik L, Klemke F, Sinnreich M, Teutloff C, Dobbek H. Angew Chem Int Ed Engl 61 e202117000 (2022)
  10. Class III hybrid cluster protein homodimeric architecture shows evolutionary relationship with Ni, Fe-carbon monoxide dehydrogenases. Fujishiro T, Takaoka K. Nat Commun 14 5609 (2023)


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