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Structure paper

TitleRational modulation of conformational fluctuations in adenylate kinase reveals a local unfolding mechanism for allostery and functional adaptation in proteins.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 106, Page 16984-16989, Year 2009
Publish dateJun 4, 2009 (structure data deposition date)
AuthorsSchrank, T.P. / Bolen, D.W. / Hilser, V.J.
External linksProc. Natl. Acad. Sci. USA / PubMed:19805185
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-3hpq:
Crystal structure of wild-type adenylate kinase from E. coli, in complex with Ap5A
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3hpr:
Crystal structure of V148G adenylate kinase from E. coli, in complex with Ap5A
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-AP5:
BIS(ADENOSINE)-5'-PENTAPHOSPHATE

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsTRANSFERASE / Enzyme Inhibitor Complex / ATP-binding / Kinase / Nucleotide biosynthesis / Nucleotide-binding

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