3MM0

Crystal structure of chimeric avidin

Summary for 3MM0

• Entry DOI: 10.2210/pdb3mm0/pdb
• Related: 1Y53 2AVI
• Descriptor: Avidin, Avidin-related protein 4/5 (2 entities in total)
• Functional Keywords: avidin, avr4, high affinity systems, hyper-thermostability, biotin binding protein
• Biological source: Gallus gallus (bantam,chickens); More
• Cellular location: Secreted: P02701
• Total number of polymer chains: 12
• Total formula weight: 172803.05

Authors

Livnah, O.,Eisenberg-Domovich, Y.,Maatta, J.A.E.,Kulomaa, M.S.,Hytonen, V.P.,Nordlund, H.R. (deposition date: 2010-04-19, release date: 2010-10-27, Last modification date: 2024-10-16)

Primary citation

Maatta, J.A.,Eisenberg-Domovich, Y.,Nordlund, H.R.,Hayouka, R.,Kulomaa, M.S.,Livnah, O.,Hytonen, V.P.
Chimeric avidin shows stability against harsh chemical conditions-biochemical analysis and 3D structure.
Biotechnol.Bioeng., 108:481-490, 2011

PubMed Abstract: Avidin and its bacterial analog streptavidin have been widely used in applications in life sciences. Recently, we described a highly thermostable engineered avidin, called chimeric avidin, which is a hybrid of avidin and avidin-related protein 4. Here, we report a protocol for pilot-scale production in E. coli and the X-ray structure of chimeric avidin. The ligand-binding properties of chimeric avidin were explored with isothermal titration calorimetry. We found chimeric avidin to be more stable against various harsh organic solvents at elevated temperatures compared to avidin and streptavidin. The properties of chimeric avidin make it a potential tool for new applications in biotechnology.

PubMed: 20939005
DOI: 10.1002/bit.22962

Experimental method

X-RAY DIFFRACTION (2.7 Å)