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Structure paper

TitleHow metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 ofThermotoga maritima.
Journal, issue, pagesJ. Biol. Chem., Vol. 294, Page 17777-17789, Year 2019
Publish dateMar 10, 2017 (structure data deposition date)
AuthorsDutoit, R. / Van Gompel, T. / Brandt, N. / Van Elder, D. / Van Dyck, J. / Sobott, F. / Droogmans, L.
External linksJ. Biol. Chem. / PubMed:31611236
MethodsX-ray diffraction
Resolution1.7 - 2 Å
Structure data

PDB-5ne6:
Crystal structure of dimeric TmPep1050 aminopeptidase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5ne7:
Crystal structure of H60A mutant of Thermotoga maritima TmPEP1050 aminopeptidase
Method: X-RAY DIFFRACTION / Resolution: 1.84 Å

PDB-5ne8:
Crystal structure of H307A mutant of Thermotoga maritima TmPEP1050 aminopeptidase
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-6nw5:
Crystal structure of TmPep1050 aminopeptidase with its metal cofactors
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-CIT:
CITRIC ACID

ChemComp-HOH:
WATER

ChemComp-ZN:
Unknown entry

ChemComp-CO:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-OH:
HYDROXIDE ION

Source
  • thermotoga maritima msb8 (bacteria)
  • thermotoga maritima (bacteria)
KeywordsLYASE / Aminopeptidase / Peptidase M42 / tetrahedral structure / metal ion binding / M42 family / HYDROLASE / M42 aminopeptidase / TET-aminopeptidase / MH clan

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