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Structure paper

TitleInsights into the structural basis of substrate recognition by histidinol-phosphate aminotransferase from Corynebacterium glutamicum
Journal, issue, pagesActa Crystallogr. ,Sect. D, Vol. 64, Page 675-685, Year 2008
Publish dateApr 2, 2008 (structure data deposition date)
AuthorsMarienhagen, J. / Sandalova, T. / Sahm, H. / Eggeling, L. / Schneider, G.
External linksActa Crystallogr. ,Sect. D / PubMed:18560156
MethodsX-ray diffraction
Resolution1.8 - 2.2 Å
Structure data

PDB-3cq4:
Histidinol-phosphate aminotransferase from Corynebacterium glutamicum
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3cq5:
Histidinol-phosphate aminotransferase from Corynebacterium glutamicum in complex with PMP
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-3cq6:
Histidinol-phosphate aminotransferase from Corynebacterium glutamicum holo-form (PLP covalently bound )
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-144:
TRIS-HYDROXYMETHYL-METHYL-AMMONIUM

ChemComp-PMP:
4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE

ChemComp-PO4:
PHOSPHATE ION

Source
  • corynebacterium glutamicum (bacteria)
KeywordsTRANSFERASE / histidinol-phosphate aminotransferase / Corynebacterium glutamicum / PLP / strep-tag / Amino-acid biosynthesis / Histidine biosynthesis / Pyridoxal phosphate / PMP

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