The backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homolog

Journal Article · Mon Oct 27 04:00:00 EDT 2008 · BMC Struct. Biol.

DOI:https://doi.org/10.1186/1472-6807-8-20· OSTI ID:1006877

Cuneo, Matthew J; Tian, Yaji; Allert, Malin; Hellinga, Homme W ^[1]

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1. Duke

We report the X-ray crystal structure of a Thermoanaerobacter tengcongensis ribose binding protein (tteRBP) determined to 1.9 {angstrom} resolution. We find that tteRBP is significantly more stable ({sup app}T{sub m} value {approx} 102 C) than the mesophilic Escherichia coli ribose binding protein (ecRBP) ({sup app}T{sub m} value {approx} 56 C). The tteRBP has essentially the identical backbone conformation (0.41 {angstrom} RMSD of 235/271 C{sub {alpha}} positions and 0.65 {angstrom} RMSD of 270/271 C{sub {alpha}} positions) as ecRBP. Classification of the amino acid substitutions as a function of structure therefore allows the identification of amino acids which potentially contribute to the observed thermal stability of tteRBP in the absence of large structural heterogeneities.

• Research Organization: Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
• Sponsoring Organization: USDOE
• OSTI ID: 1006877
• Journal Information: BMC Struct. Biol., Journal Name: BMC Struct. Biol. Journal Issue: 03, 2008 Vol. 8
• Country of Publication: United States
• Language: ENGLISH

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
60 APPLIED LIFE SCIENCES
AMINO ACIDS
BACTERIA
CLASSIFICATION
CRYSTAL STRUCTURE
ESCHERICHIA COLI
FUNCTIONS
PROTEINS
RESOLUTION
RIBOSE
STABILITY