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Structure paper

TitleThe structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases.
Journal, issue, pagesMBio, Vol. 2, Year 2011
Publish dateAug 31, 2011 (structure data deposition date)
AuthorsLovering, A.L. / Capeness, M.J. / Lambert, C. / Hobley, L. / Sockett, R.E.
External linksMBio / PubMed:21990613
MethodsX-ray diffraction
Resolution1.28 - 2.641 Å
Structure data

PDB-3tm8:
Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus
Method: X-RAY DIFFRACTION / Resolution: 1.28 Å

PDB-3tmb:
Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-3tmc:
Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-3tmd:
Bd1817, a HDG"Y"P protein from Bdellovibrio bacteriovorus
Method: X-RAY DIFFRACTION / Resolution: 2.641 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-FE:
Unknown entry

ChemComp-DMS:
DIMETHYL SULFOXIDE / DMSO, precipitant*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • bdellovibrio bacteriovorus (bacteria)
KeywordsHYDROLASE / SIGNALING PROTEIN / HD-GYP / phosphodiesterase / UNKNOWN FUNCTION

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