Structures of mesophilic and extremophilic citrate synthases reveal rigidity and flexibility for function.

Wells, Stephen A; Crennell, Susan J; Danson, Michael J

Wells, Stephen A; Crennell, Susan J; Danson, Michael J.

Affiliation

Wells SA; Department of Chemistry/Department of Physics, University of Bath, BATH, BA2 7AY, United Kingdom.

Proteins ; 82(10): 2657-70, 2014 Oct.

Article in En | MEDLINE | ID: mdl-24948467

Subject(s)

Bacterial Proteins/chemistry; Citrate (si)-Synthase/chemistry; Models, Molecular; Animals; Arthrobacter/enzymology; Arthrobacter/growth & development; Bacillus subtilis/enzymology; Bacterial Proteins/metabolism; Binding Sites; Catalytic Domain; Citrate (si)-Synthase/metabolism; Databases, Protein; Enzyme Stability; Hydrophobic and Hydrophilic Interactions; Ligands; Molecular Dynamics Simulation; Protein Conformation; Pyrobaculum/enzymology; Pyrobaculum/growth & development; Pyrococcus furiosus/enzymology; Pyrococcus furiosus/growth & development; Sulfolobus solfataricus/enzymology; Sulfolobus solfataricus/growth & development; Sus scrofa; Thermoplasma/enzymology; Thermoplasma/growth & development; Thermus thermophilus/enzymology; Thermus thermophilus/growth & development

Key words

Elnemo; FIRST; FRODA; elastic network; flexible motion; geometric simulation; psychrophile; rigidity; thermophile

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Models, Molecular / Citrate (si)-Synthase Limits: Animals Language: En Journal: Proteins Journal subject: BIOQUIMICA Year: 2014 Type: Article Affiliation country: United kingdom

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