7CQ0
Crystal structure of Streptoavidin-C1 from Streptomyces cinamonensis
7CQ0 の概要
| エントリーDOI | 10.2210/pdb7cq0/pdb |
| 分子名称 | Mature Streptoavidin-C1 (2 entities in total) |
| 機能のキーワード | avidin, antifungal, biotin, antimicrobial protein |
| 由来する生物種 | Streptomyces sp. H036 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 20172.20 |
| 構造登録者 | Jeon, B.J.,Kim, S.,Lee, J.-H.,Kim, M.S.,Hwang, K.Y. (登録日: 2020-08-08, 公開日: 2021-07-14, 最終更新日: 2023-11-29) |
| 主引用文献 | Jeon, B.J.,Kim, S.,Kim, M.S.,Lee, J.H.,Kim, B.S.,Hwang, K.Y. 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. Iucrj, 8:168-177, 2021 Cited by PubMed Abstract: The members of the avidin protein family are well known for their high affinity towards d-biotin and their structural stability. These properties make avidins a valuable tool for various biotechnological applications. In the present study, two avidin-like biotin-binding proteins (named streptavidin C1 and C2) from were newly identified while exploring antifungal proteins against f. sp. . Streptavidin C1 reveals a low correlation (a sequence identity of approximately 64%) with all known streptavidins, whereas streptavidin C2 shares a sequence identity of approximately 94% with other streptavidins. Here, the crystal structures of streptavidin C1 in the mature form and in complex with biotin at 2.1 and 2.5 Å resolution, respectively, were assessed. The overall structures present similar tetrameric features with symmetry to other (strept)avidin structures. Interestingly, the long C-terminal region comprises a short α-helix (C-Lid; residues 169-179) and an extension C-terminal peptide (ECP; residues 180-191) which stretches into the biotin-binding sites of the same monomer. This ECP sequence (-VTSANPPAS-) is a newly defined biotin-binding site, which reduces the ability to bind to (strept)avidin family proteins. The novel streptavidin C1 could help in the development of an engineered tetrameric streptavidin with reduced biotin-binding capacity as well as other biomaterial tools. PubMed: 33708394DOI: 10.1107/S2052252520015675 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.03 Å) |
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