Structural analysis of the elongation factor G protein from the low-temperature-adapted bacterium Arthrobacter globiformis SI55.

Berchet, V; Thomas, T; Cavicchioli, R; Russell, N J; Gounot, A M

Berchet, V; Thomas, T; Cavicchioli, R; Russell, N J; Gounot, A M.

Affiliation

Berchet V; Ecologie Microbienne, UMR CNRS 5557, Université Lyon I, Villeurbanne, France.

Extremophiles ; 4(2): 123-30, 2000 Apr.

Article in En | MEDLINE | ID: mdl-10805567

Subject(s)

Amino Acid Sequence/genetics; Arthrobacter/genetics; Bacterial Proteins/genetics; Cold Climate; Peptide Elongation Factor G/genetics; Bacterial Proteins/chemistry; Micrococcus luteus/genetics; Models, Molecular; Molecular Sequence Data; Mycobacterium tuberculosis/genetics; Peptide Elongation Factor G/chemistry; Protein Structure, Tertiary; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Structure-Activity Relationship

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Collection: 01-internacional Database: MEDLINE Main subject: Arthrobacter / Bacterial Proteins / Amino Acid Sequence / Cold Climate / Peptide Elongation Factor G Type of study: Prognostic_studies Language: En Journal: Extremophiles Journal subject: BIOLOGIA Year: 2000 Document type: Article Affiliation country: France Country of publication: Germany

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