7PZO

mite allergen Der p 3 from Dermatophagoides pteronyssinus

7PZO の概要

• エントリーDOI: 10.2210/pdb7pzo/pdb
• 分子名称: mite allergen Der p 3, SULFATE ION (3 entities in total)
• 機能のキーワード: allergen
• 由来する生物種: Dermatophagoides pteronyssinus (European house dust mite)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49930.44

構造登録者

Timofeev, V.I.,Shevtsov, M.B.,Abramchik, Y.A.,Mikheeva, O.O.,Kostromina, M.A.,Lykoshin, D.D.,Zayats, E.A.,Zavriev, S.K.,Esipov, R.S.,Kuranova, I.P. (登録日: 2021-10-13, 公開日: 2022-11-02, 最終更新日: 2024-01-31)

主引用文献

Timofeev, 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.
Structural plasticity and thermal stability of the histone-like protein from Spiroplasma melliferum are due to phenylalanine insertions into the conservative scaffold.
J.Biomol.Struct.Dyn., 36:4392-4404, 2018

PubMed Abstract: The histone-like (HU) protein is one of the major nucleoid-associated proteins of the bacterial nucleoid, which shares high sequence and structural similarity with IHF but differs from the latter in DNA-specificity. Here, we perform an analysis of structural-dynamic properties of HU protein from Spiroplasma melliferum and compare its behavior in solution to that of another mycoplasmal HU from Mycoplasma gallisepticum. The high-resolution heteronuclear NMR spectroscopy was coupled with molecular-dynamics study and comparative analysis of thermal denaturation of both mycoplasmal HU proteins. We suggest that stacking interactions in two aromatic clusters in the HUSpm dimeric interface determine not only high thermal stability of the protein, but also its structural plasticity experimentally observed as slow conformational exchange. One of these two centers of stacking interactions is highly conserved among the known HU and IHF proteins. Second aromatic core described recently in IHFs and IHF-like proteins is considered as a discriminating feature of IHFs. We performed an electromobility shift assay to confirm high affinities of HUSpm to both normal and distorted dsDNA, which are the characteristics of HU protein. MD simulations of HUSpm with alanine mutations of the residues forming the non-conserved aromatic cluster demonstrate its role in dimer stabilization, as both partial and complete distortion of the cluster enhances local flexibility of HUSpm.

PubMed: 29283021
DOI: 10.1080/07391102.2017.1417162

実験手法

X-RAY DIFFRACTION (2.25 Å)