8R2C

Crystal structure of the Vint domain from Tetrahymena thermophila

Summary for 8R2C

• Entry DOI: 10.2210/pdb8r2c/pdb
• Descriptor: von willebrand factor type A (VWA) domain was originally protein, SULFATE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: hedgehog, vint, intein, hint, von willebrand factor type a domain, unknown function
• Biological source: Tetrahymena thermophila SB210
• Total number of polymer chains: 1
• Total formula weight: 19947.80

Authors

Iwai, H.,Beyer, H.M.,Johannson, J.E.,Li, M.,Wlodawer, A. (deposition date: 2023-11-03, release date: 2024-02-28, Last modification date: 2024-05-01)

Primary citation

Iwai, H.,Beyer, H.M.,Johansson, J.E.M.,Li, M.,Wlodawer, A.
The three-dimensional structure of the Vint domain from Tetrahymena thermophila suggests a ligand-regulated cleavage mechanism by the HINT fold.
Febs Lett., 598:864-874, 2024

PubMed Abstract: Vint proteins have been identified in unicellular metazoans as a novel hedgehog-related gene family, merging the von Willebrand factor type A domain and the Hedgehog/INTein (HINT) domains. We present the first three-dimensional structure of the Vint domain from Tetrahymena thermophila corresponding to the auto-processing domain of hedgehog proteins, shedding light on the unique features, including an adduct recognition region (ARR). Our results suggest a potential binding between the ARR and sulfated glycosaminoglycans like heparin sulfate. Moreover, we uncover a possible regulatory role of the ARR in the auto-processing by Vint domains, expanding our understanding of the HINT domain evolution and their use in biotechnological applications. Vint domains might have played a crucial role in the transition from unicellular to multicellular organisms.

PubMed: 38351630
DOI: 10.1002/1873-3468.14817

Experimental method

X-RAY DIFFRACTION (1.8 Å)