7CQ0

Crystal structure of Streptoavidin-C1 from Streptomyces cinamonensis

Summary for 7CQ0

• Entry DOI: 10.2210/pdb7cq0/pdb
• Descriptor: Mature Streptoavidin-C1 (2 entities in total)
• Functional Keywords: avidin, antifungal, biotin, antimicrobial protein
• Biological source: Streptomyces sp. H036
• Total number of polymer chains: 1
• Total formula weight: 20172.20

Authors

Jeon, B.J.,Kim, S.,Lee, J.-H.,Kim, M.S.,Hwang, K.Y. (deposition date: 2020-08-08, release date: 2021-07-14, Last modification date: 2023-11-29)

Primary citation

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

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: 33708394
DOI: 10.1107/S2052252520015675

Experimental method

X-RAY DIFFRACTION (2.03 Å)