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Literature summary for 3.2.1.6 extracted from

  • Bleicher, L.; Prates, E.T.; Gomes, T.C.; Silveira, R.L.; Nascimento, A.S.; Rojas, A.L.; Golubev, A.; Martinez, L.; Skaf, M.S.; Polikarpov, I.
    Molecular basis of the thermostability and thermophilicity of laminarinases: X-ray structure of the hyperthermostable laminarinase from Rhodothermus marinus and molecular dynamics simulations (2011), J. Phys. Chem. B, 115, 7940-7949.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Rhodothermus marinus

Crystallization (Commentary)

Crystallization (Comment) Organism
to 1.95 A resolution, and molecular dynamics simulation studies. LamR is formed mostly by beta-sheets in a complex jelly roll topology that is conserved among members of glycosyl hydrolase family 16. It contains a relatively large number of salt bridges, which are not randomly distributed on the structure. They form clusters interconnecting beta-sheets of the catalytic domain. Structure reveals a glycerol molecule fortuitously bound to the active site of the enzyme molecule Rhodothermus marinus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ identification of calcium ions bound to each monomer, in equivalent sites of each polypeptide chain in the asymmetric unit cell, and displaying the same coordination patterns. Coordination of the calcium ion is 6fold, and involves Gly60 of main chain, Asp248, main chain and side chain, Glu18 of main chain, and two water molecules. Crystallization data Rhodothermus marinus

Organism

Organism UniProt Comment Textmining
Rhodothermus marinus O52754 member of glycosyl hydrolase family 16
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Synonyms

Synonyms Comment Organism
LamR
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Rhodothermus marinus