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Structure paper

TitleMechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex.
Journal, issue, pagesNature, Vol. 414, Page 325-329, Year 2001
Publish dateSep 3, 2001 (structure data deposition date)
AuthorsLake, M.W. / Wuebbens, M.M. / Rajagopalan, K.V. / Schindelin, H.
External linksNature / PubMed:11713534
MethodsX-ray diffraction
Resolution1.7 - 2.9 Å
Structure data

PDB-1jw9:
Structure of the Native MoeB-MoaD Protein Complex
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1jwa:
Structure of the ATP-bound MoeB-MoaD Protein Complex
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-1jwb:
Structure of the Covalent Acyl-Adenylate Form of the MoeB-MoaD Protein Complex
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

Source
  • escherichia coli (E. coli)
KeywordsLIGASE / MoeB: modified Rossmann fold; (2) Cys-X-X-Cys Zinc-binding motifs; MoaD: ubiquitin-like fold / MoeB: modified Rossmann fold; MoaD: ubiquitin-like fold

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