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Structure paper

TitleStructural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold.
Journal, issue, pagesJ. Biomol. Struct. Dyn., Vol. 36, Page 4392-4404, Year 2018
Publish dateJul 13, 2017 (structure data deposition date)
AuthorsTimofeev, V.I. / Altukhov, D.A. / Talyzina, A.A. / Agapova, Y.K. / Vlaskina, A.V. / Korzhenevskiy, D.A. / Kleymenov, S.Y. / Bocharov, E.V. / Rakitina, T.V.
External linksJ. Biomol. Struct. Dyn. / PubMed:29283021
MethodsNMR (solution) / X-ray diffraction
Resolution2.25 Å
Structure data

PDB-5ogu:
Structure of DNA-binding HU protein from micoplasma Spiroplasma melliferum
Method: SOLUTION NMR

PDB-7pzo:
mite allergen Der p 3 from Dermatophagoides pteronyssinus
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • spiroplasma melliferum kc3 (bacteria)
  • dermatophagoides pteronyssinus (European house dust mite)
KeywordsDNA BINDING PROTEIN / ALLERGEN

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