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Structure paper

TitleGuanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme.
Journal, issue, pagesProtein Sci., Vol. 15, Page 853-861, Year 2006
Publish dateNov 17, 2005 (structure data deposition date)
AuthorsYousef, M.S. / Bischoff, N. / Dyer, C.M. / Baase, W.A. / Matthews, B.W.
External linksProtein Sci. / PubMed:16600969
MethodsX-ray diffraction
Resolution1.45 - 1.8 Å
Structure data

PDB-2f2q:
High resolution crystal structure of T4 lysozyme mutant L20R63/A liganded to guanidinium ion
Method: X-RAY DIFFRACTION / Resolution: 1.45 Å

PDB-2f32:
Xray crystal structure of lysozyme mutant L20/R63A liganded to ethylguanidinium
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

PDB-2f47:
Xray crystal structure of T4 lysozyme mutant L20/R63A liganded to methylguanidinium
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-CL:
Unknown entry

ChemComp-GAI:
GUANIDINE

ChemComp-HED:
2-HYDROXYETHYL DISULFIDE

ChemComp-HOH:
WATER

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-EGD:
N-ETHYLGUANIDINE

ChemComp-MGX:
1-METHYLGUANIDINE

Source
  • enterobacteria phage t4 (virus)
KeywordsHYDROLASE / MOLECULAR SWITCH / T4 LYSOZYME / NANO-BITECHNOLOGY / PROTEIN ENGINEERING / PROTEIN DESIGN

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