Tadej Satler (Avtor), San Hadži (Avtor), Roman Jerala (Avtor)

Povzetek

Coiled-coil protein origami (CCPO) uses modular coiled-coil building blocks and topological principles to design polyhedral structures distinct from those of natural globular proteins. While the CCPO strategy has proven successful in designing diverse protein topologies, no high-resolution structural information has been available about these novel protein folds. Here we report the crystal structure of a single-chain CCPO in the shape of a triangle. While neither cyclization nor the addition of nanobodies enabled crystallization, it was ultimately facilitated by the inclusion of a GCN$_2$ homodimer. Triangle edges are formed by the orthogonal parallel coiled-coil dimers P1:P2, P3:P4, and GCN$_2$ connected by short linkers. A triangle has a large central cavity and is additionally stabilized by side-chain interactions between neighboring segments at each vertex. The crystal lattice is densely packed and stabilized by a large number of contacts between triangles. Interestingly, the polypeptide chain folds into a trefoil-type protein knot topology, and AlphaFold2 fails to predict the correct fold. The structure validates the modular CC-based protein design strategy, providing molecular insight underlying CCPO stabilization and new opportunities for the design.

Ključne besede

biokemija;proteinski origami;obvite vijačnice;CCPO;DNK;

Podatki

Jezik: Angleški jezik
Leto izida:
Tipologija: 1.01 - Izvirni znanstveni članek
Organizacija: KI - Kemijski inštitut
Založnik: American Chemical Society
UDK: 577
COBISS: 169812995 Povezava se bo odprla v novem oknu
ISSN: 1520-5126
Št. ogledov: 13
Št. prenosov: 4
Ocena: 0 (0 glasov)
Metapodatki: JSON JSON-RDF JSON-LD TURTLE N-TRIPLES XML RDFA MICRODATA DC-XML DC-RDF RDF

Ostali podatki

Sekundarni jezik: Slovenski jezik
Sekundarne ključne besede: biokemija;proteinski origami;obvite vijačnice;CCPO;DNK;
Vrsta dela (COBISS): Članek v reviji
Komentar vira: Nasl. z nasl. zaslona; Opis vira z dne 25. 10. 2023;
Strani: str. 16995–17000
Letnik: ǂVol. ǂ145
Zvezek: ǂiss. ǂ31
Čas izdaje: Aug. 9, 2023
DOI: 10.1021/jacs.3c05531
ID: 21439512