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Literature summary for 3.2.1.B26 extracted from

  • Aguilar, C.F.
    Sanderson, I.; Moracci, M.; Ciaramella, M.; Nucci, R.; Rossi, M.; Pearl, L.H.: Crystal structure of the beta-glycosidase from the hyperthermophilic archeon Sulfolobus solfataricus: resilience as a key factor in thermostability (1997), J. Mol. Biol., 271, 789-802.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
the crystal structure is determined using multiple isomorphous replacement assisted by solvent flattening, histogram equalisation and non-crystallographic symmetry averaging, and refined at 2.6 A resolution. the enzyme crystallises as a tetramer with 222 point group symmetry, one dyad of which is crystallographic, with a dimer in the asymmetric unit. Analysis of the structure reveals two features which differ significantly from mesophile proteins: (1) an unusually large proportion of surface ion-pairs involved in networks that cross-link sequentially separate structures on the protein surface, and (2) an unusually large number of solvent molecules buried in hydrophilic cavities between sequentially separate structures in the protein core. These factors suggest a model for hyperthermostability via resilience rather than rigidity Saccharolobus solfataricus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
4 * 60000 Saccharolobus solfataricus
220000
-
glycerol gradient centrifugation Saccharolobus solfataricus
240000
-
gel filtration Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus
-
-
-

Subunits

Subunits Comment Organism
tetramer 4 * 60000 Saccharolobus solfataricus