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Structure paper

TitleBiochemical and Structural Studies of a HECT-like Ubiquitin Ligase from Escherichia coli O157:H7.
Journal, issue, pagesJ. Biol. Chem., Vol. 286, Page 441-449, Year 2011
Publish dateJun 2, 2010 (structure data deposition date)
AuthorsLin, D.Y. / Diao, J. / Zhou, D. / Chen, J.
External linksJ. Biol. Chem. / PubMed:20980253
MethodsX-ray diffraction
Resolution2.1 - 2.5 Å
Structure data

PDB-3naw:
Crystal structure of E. coli O157:H7 effector protein NleL
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3nb2:
Crystal structure of E. coli O157:H7 effector protein NleL
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-GOL:
GLYCEROL

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

ChemComp-HOH:
WATER

ChemComp-DTT:
2,3-DIHYDROXY-1,4-DITHIOBUTANE

Source
  • escherichia coli (E. coli)
KeywordsLIGASE / effector protein / pentapeptide / HECT domain / HECT E3 ubiquitin ligase / secreted effector protein

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