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(A) Multiple sequence alignment of the avidin family

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posted on 30.12.2011 by Vesa P Hytönen, Juha AE Määttä, Heidi Kidron, Katrin K Halling, Jarno Hörhä, Tuomas Kulomaa, Thomas KM Nyholm, Mark S Johnson, Tiina A Salminen, Markku S Kulomaa, Tomi T Airenne

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Taken from "Avidin related protein 2 shows unique structural and functional features among the avidin protein family"

BMC Biotechnology 2005;5():28-28.

Published online 7 Oct 2005

PMCID:PMC1282572.

Copyright © 2005 Hytönen et al; licensee BioMed Central Ltd.

The secondary structure elements are numbered according to the AVR2 structure. The residues mutated in this study (AVR2, Ile-109; AVR4, Lys-109; AVR6, Cys-58) are coloured green. Residue Cys-122 in AVR4, which was mutated to serine in a previous study [36], is indicated in blue. (B) Two tetramers found in the asymmetric unit of the AVR2-b crystal. (C) Monomer A of AVR2-b. The weighted difference – electron density map (blue), calculated in the absence of biotin, is drawn with a 1.5 Å radius around the atoms of D-biotin of the final structure of AVR2-b. Contours are shown at 3.0σ. The secondary structure elements of AVR2-b are numbered. (D) A close-up view of (C) focused on biotin.

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