4BJ8

Zebavidin

4BJ8 の概要

• エントリーDOI: 10.2210/pdb4bj8/pdb
• 分子名称: ZEBAVIDIN, BIOTIN, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: biotin-binding protein
• 由来する生物種: DANIO RERIO (ZEBRAFISH)
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 221685.09

構造登録者

Airenne, T.T.,Parthiban, M.,Niederhauser, B.,Zmurko, J.,Kulomaa, M.S.,Hytonen, V.P.,Johnson, M.S. (登録日: 2013-04-17, 公開日: 2013-11-20, 最終更新日: 2024-10-23)

主引用文献

Niederhauser, B.,Zmurko, J.,Parthiban, M.,Ojanen, M.,Kukkurainen, S.,Maatta, J.A.E.,Leppiniemi, J.,Janis, J.,Parikka, M.,Turpeinen, H.,Pesu, M.,Johnson, M.S.,Airenne, T.T.,Kulomaa, M.S.,Hytonen, V.P.
Zebavidin
Plos One, 8:77207-, 2013

PubMed Abstract: The avidin protein family members are well known for their high affinity towards D-biotin and high structural stability. These properties make avidins valuable tools for a wide range of biotechnology applications. We have identified a new member of the avidin family in the zebrafish (Danio rerio) genome, hereafter called zebavidin. The protein is highly expressed in the gonads of both male and female zebrafish and in the gills of male fish, but our data suggest that zebavidin is not crucial for the developing embryo. Biophysical and structural characterisation of zebavidin revealed distinct properties not found in any previously characterised avidins. Gel filtration chromatography and native mass spectrometry suggest that the protein forms dimers in the absence of biotin at low ionic strength, but assembles into tetramers upon binding biotin. Ligand binding was analysed using radioactive and fluorescently labelled biotin and isothermal titration calorimetry. Moreover, the crystal structure of zebavidin in complex with biotin was solved at 2.4 Å resolution and unveiled unique ligand binding and subunit interface architectures; the atomic-level details support our physicochemical observations.

PubMed: 24204770
DOI: 10.1371/JOURNAL.PONE.0077207

実験手法

X-RAY DIFFRACTION (2.4 Å)