Iron superoxide dismutase from the archaeon Sulfolobus sulfataricus : Analysis of structure and thermostability.

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Iron superoxide dismutase from the archaeon Sulfolobus sulfataricus : Analysis of structure and thermostability. / Ursby, Thomas; Adinolfi, Bianca Stella; Al-Karadaghi, Salam; De Vendittis, Emmanuele; Buccini, Vincenzo.

In: Journal of Molecular Biology, Vol. 286, No. 1, 1999, p. 189-205.

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Ursby, Thomas ; Adinolfi, Bianca Stella ; Al-Karadaghi, Salam ; De Vendittis, Emmanuele ; Buccini, Vincenzo. / Iron superoxide dismutase from the archaeon Sulfolobus sulfataricus : Analysis of structure and thermostability. In: Journal of Molecular Biology. 1999 ; Vol. 286, No. 1. pp. 189-205.

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TY - JOUR

T1 - Iron superoxide dismutase from the archaeon Sulfolobus sulfataricus : Analysis of structure and thermostability.

AU - Ursby, Thomas

AU - Adinolfi, Bianca Stella

AU - Al-Karadaghi, Salam

AU - De Vendittis, Emmanuele

AU - Buccini, Vincenzo

PY - 1999

Y1 - 1999

N2 - The crystal structure of superoxide dismutase (SOD) from the hyper thermophile Sulfolobus solfataricus has been determined at 2.3 Å resolution by molecular replacement and refined to a crystallographic R-factor of 16.8 % (Rfree 19.8 %). The crystals belong to the space group C2 (a = 76.3 Å, b = 124.3 Å,c = 60.3 Å, β = 128.8°) with two identical monomers in the asymmetric unit. The monomer has a molecular weight of 24 kDa and consists of 210 amino acid residues of which 205 are visible in the electron density map. The overall fold of the monomer of S. solfataricus SOD is similar to that of the other known Fe or Mn-SODs. S. solfataricus SOD forms a very compact tetramer of a type similar to that of SOD from the hyperthermophile Aquifex pyrophilus. Both structures show an elevated number of inter-subunit ion-pairs compared with the mesophilic SOD from Mycobacterium tuberculosis and the thermophilic SOD from Thermus thermophilus. However, in contrast to the A. pyrophilus SOD structure, the number of intra-subunit ion-pairs as well as inter-subunit hydrogen bonds is not higher than in the compared mesophilic and thermophilic SOD structures. The electron density also revealed an unexpected and unusual covalent modification of a conserved tyrosine in the active site. Its involvement in the specific activity of the enzyme is discussed.

AB - The crystal structure of superoxide dismutase (SOD) from the hyper thermophile Sulfolobus solfataricus has been determined at 2.3 Å resolution by molecular replacement and refined to a crystallographic R-factor of 16.8 % (Rfree 19.8 %). The crystals belong to the space group C2 (a = 76.3 Å, b = 124.3 Å,c = 60.3 Å, β = 128.8°) with two identical monomers in the asymmetric unit. The monomer has a molecular weight of 24 kDa and consists of 210 amino acid residues of which 205 are visible in the electron density map. The overall fold of the monomer of S. solfataricus SOD is similar to that of the other known Fe or Mn-SODs. S. solfataricus SOD forms a very compact tetramer of a type similar to that of SOD from the hyperthermophile Aquifex pyrophilus. Both structures show an elevated number of inter-subunit ion-pairs compared with the mesophilic SOD from Mycobacterium tuberculosis and the thermophilic SOD from Thermus thermophilus. However, in contrast to the A. pyrophilus SOD structure, the number of intra-subunit ion-pairs as well as inter-subunit hydrogen bonds is not higher than in the compared mesophilic and thermophilic SOD structures. The electron density also revealed an unexpected and unusual covalent modification of a conserved tyrosine in the active site. Its involvement in the specific activity of the enzyme is discussed.

KW - superoxide dismutase

KW - Sulfolobus solfataricus

KW - X-ray structure

KW - thermostability

KW - tyrosine modification

U2 - 10.1006/jmbi.1998.2471

DO - 10.1006/jmbi.1998.2471

M3 - Article

VL - 286

SP - 189

EP - 205

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 1089-8638

IS - 1

ER -