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pro vyhledávání: '"Martina Wenk"'
Autor:
Martina Wenk, Rainer Jaenicke
Publikováno v:
Journal of Molecular Biology. 293:117-124
The betagamma-crystallin superfamily consists of a class of homologous two-domain proteins with Greek-key fold. Protein S, a Ca(2+)-binding spore-coat protein from the soil bacterium Myxococcus xanthus exhibits a high degree of sequential and structu
Autor:
Tad A. Holak, Robert Huber, Martina Wenk, Eva-Maria Mayr, Rainer Jaenicke, Roland Baumgartner
Publikováno v:
Journal of Molecular Biology. 286:1533-1545
Protein S from Myxococcus xanthus is a member of the βγ-crystallin superfamily. Its N and C-terminal domains (NPS and CPS, respectively) show a high degree of structural similarity and possess the capacity to bind two calcium ions per domain. For N
Autor:
Eva-Maria Mayr, Martina Wenk
Publikováno v:
European Journal of Biochemistry. 255:604-610
Protein S, a calcium-binding spore coat protein from the soil bacterium Myxococcus xanthus, belongs to a group of structurally related proteins, the betagamma-crystallin superfamily. Common features of this protein family are the Greek-key structural
Publikováno v:
FEBS Letters. (1-2):127-130
Protein S, a two-domain spore coat protein from Myxococcus xanthus, is structurally related to eye-lens βγ-crystallins. No natural monomeric one-domain member of this protein superfamily is known. To determine the stability of the single domains an