4BJ8

Zebavidin

Summary for 4BJ8

• Entry DOI: 10.2210/pdb4bj8/pdb
• Descriptor: ZEBAVIDIN, BIOTIN, GLYCEROL, ... (4 entities in total)
• Functional Keywords: biotin-binding protein
• Biological source: DANIO RERIO (ZEBRAFISH)
• Total number of polymer chains: 16
• Total formula weight: 221685.09

Authors

Airenne, T.T.,Parthiban, M.,Niederhauser, B.,Zmurko, J.,Kulomaa, M.S.,Hytonen, V.P.,Johnson, M.S. (deposition date: 2013-04-17, release date: 2013-11-20, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)