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Structure paper

TitleX-ray studies on ternary complexes of maltodextrin phosphorylase.
Journal, issue, pagesArch. Biochem. Biophys., Vol. 471, Page 11-19, Year 2008
Publish dateAug 29, 2005 (structure data deposition date)
AuthorsCampagnolo, M. / Campa, C. / Zorzi, R.D. / Wuerges, J. / Geremia, S.
External linksArch. Biochem. Biophys. / PubMed:18164678
MethodsX-ray diffraction
Resolution2.01 - 2.2 Å
Structure data

PDB-2av6:
X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family
Method: X-RAY DIFFRACTION / Resolution: 2.01 Å

PDB-2aw3:
X-Ray studies on maltodextrin phosphorylase complexes: recognition of substrates and cathalitic mechanism of phosphorylase family
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2azd:
X-Ray studies on Maltodextrin Phosphorylase (MalP) Complexes: recognition of substrates and CATALYTIC mechanism of phosphorylase family
Method: X-RAY DIFFRACTION / Resolution: 2.16 Å

Chemicals

ChemComp-NO3:
NITRATE ION

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-VO4:
VANADATE ION

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / maltopentaose / carbohydrate recognition / phosphorylase mechanism / ternary complexes with natural and inhibitory substrates

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