3t2w

Crystal structure of shwanavidin (F43A) - biotin complex

spinqualitylabelsall models 3t2w, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3t2w is a 1 chain structure with sequence from Shewanella denitrificans OS217. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: BTN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q12QS6_SHEDO Publication Abstract from PubMed Shwanavidin is an avidin-like protein from the marine proteobactrium Shewanella denitrificans, which exhibits an innate dimeric structure while maintaining high affinity towards biotin. A unique residue (Phe-43) from the L3,4 loop and a distinctive disulfide bridge were shown to account for the high affinity towards biotin. Phe-43 emulates the function and position of the critical intermonomeric Trp that characterizes the tetrameric avidins but is lacking in shwanavidin. The 18 copies of the apo monomer revealed distinctive snapshots of L3,4 and Phe-43, providing rare insight into loop flexibility, binding-site accessibility and psychrophilic adaptation. Nevertheless, as in all avidins, shwanavidin also displays high thermostability properties. The unique features of shwanavidin may provide a platform for the design of a long-sought-after monovalent form of avidin, which would be ideal for novel types of biotechnological application. Structural Adaptation of a Thermostable Biotin-Binding Protein in a Psychrophilic Environment.,Meir A, Bayer EA, Livnah O J Biol Chem. 2012 Apr 5. PMID:22493427 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Avidin 3D structures

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