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TitleNative Alanine Substitution in the Glycine Hinge Modulates Conformational Flexibility of Heme Nitric Oxide/Oxygen (H-NOX) Sensing Proteins.
Journal, issue, pagesACS Chem. Biol., Vol. 13, Page 1631-1639, Year 2018
Publish dateOct 22, 2017 (structure data deposition date)
AuthorsHespen, C.W. / Bruegger, J.J. / Guo, Y. / Marletta, M.A.
External linksACS Chem. Biol. / PubMed:29757599
MethodsX-ray diffraction
Resolution1.641 - 1.901 Å
Structure data

PDB-6bdd:
Crystal structure of Fe(II) unliganded H-NOX protein from K. algicida
Method: X-RAY DIFFRACTION / Resolution: 1.901 Å

PDB-6bde:
Crystal structure of Fe(II) unliganded H-NOX protein mutant A71G from K. algicida
Method: X-RAY DIFFRACTION / Resolution: 1.641 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-HOH:
WATER

Source
  • kordia algicida ot-1 (bacteria)
KeywordsSIGNALING PROTEIN / Nitric oxide signaling / heme nitric oxide/oxygen sensing protein

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