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TitleStructural basis of functional diversification of the HD-GYP domain revealed by the Pseudomonas aeruginosa PA4781 protein, which displays an unselective bimetallic binding site.
Journal, issue, pagesJ. Bacteriol., Vol. 197, Page 1525-1535, Year 2015
Publish dateSep 3, 2014 (structure data deposition date)
AuthorsRinaldo, S. / Paiardini, A. / Stelitano, V. / Brunotti, P. / Cervoni, L. / Fernicola, S. / Protano, C. / Vitali, M. / Cutruzzola, F. / Giardina, G.
External linksJ. Bacteriol. / PubMed:25691523
MethodsX-ray diffraction
Resolution2.2 Å
Structure data

PDB-4r8z:
Crystal Structure of PA4781 HD-GYP domain from Pseudomonas aeruginosa at 2.2A resolution showing a bi-metallic Ni ion center
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-NI:
NICKEL (II) ION

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

Source
  • pseudomonas aeruginosa pao1 (bacteria)
KeywordsHYDROLASE / bimetallic / c-di-GMP / PDE / phosphdiesterase / cyclic-di-GMP / biofilm

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