Insights into the structure of mature streptavidin C1 from Streptomyces cinnamonensis reveal the self-binding of the extension C-terminal peptide to biotin-binding sites

Jeon, B.J.; Kim, S.; Kim, M.-S.; Lee, J.-H.; Kim, B.S.; Hwang, K.Y.

doi:10.1107/S2052252520015675

Figure 4
Enlarged view of the streptavidin C1 structure complexed with biotin. The hydrogen-bonding network with biotin is formed by Asn56, Ser60, Tyr76, Ser78 and Asp160, and hydrophobic interactions occur between biotin and strictly conserved residues (Leu58 in Loop^1–2, Val80 in Loop^3–4, Tyr111 in Loop^5–6, Trp140 in β7 and Leu142 in β7). Residues in the flexible Loop^3–4 (–⁸⁰VGN⁸²–) play a pivotal role in the binding of biotin, which is mainly formed with Trp152 (Mol C) in a closed conformation.

IUCrJ

Volume 8| Part 2| March 2021| Pages 168-177

ISSN: 2052-2525

https://doi.org/10.1107/S2052252520015675

BIOLOGY | MEDICINE

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