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-Structure paper
Title | The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases. |
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Journal, issue, pages | MBio, Vol. 2, Year 2011 |
Publish date | Aug 31, 2011 (structure data deposition date) |
Authors | Lovering, A.L. / Capeness, M.J. / Lambert, C. / Hobley, L. / Sockett, R.E. |
External links | MBio / PubMed:21990613 |
Methods | X-ray diffraction |
Resolution | 1.28 - 2.641 Å |
Structure data | PDB-3tm8: PDB-3tmb: PDB-3tmc: PDB-3tmd: |
Chemicals | ChemComp-PO4: ChemComp-FE: ChemComp-DMS: ChemComp-EDO: ChemComp-HOH: |
Source |
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Keywords | HYDROLASE / SIGNALING PROTEIN / HD-GYP / phosphodiesterase / UNKNOWN FUNCTION |