Crystal structure of TM1367 from Thermotoga maritima at 1.90 A resolution reveals an atypical member of the cyclophilin (peptidylprolyl isomerase) fold

Proteins. 2006 Jun 1;63(4):1112-8. doi: 10.1002/prot.20894.
No abstract available

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Binding Sites
  • Crystallography, X-Ray
  • Cyclophilins / chemistry*
  • Cyclophilins / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Peptidylprolyl Isomerase / chemistry*
  • Peptidylprolyl Isomerase / classification
  • Peptidylprolyl Isomerase / metabolism*
  • Polyethylene Glycols
  • Protein Folding
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Thermotoga maritima / enzymology*

Substances

  • Bacterial Proteins
  • Polyethylene Glycols
  • Cyclophilins
  • Peptidylprolyl Isomerase