7WF8

Crystal structure of mouse SNX25 RGS domain in space group P212121

Summary for 7WF8

• Entry DOI: 10.2210/pdb7wf8/pdb
• Descriptor: Sorting nexin-25, GLYCEROL, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• Functional Keywords: sorting nexin, snx25, rgs, protein transport
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 2
• Total formula weight: 32674.45

Authors

Zhang, Y.,Xu, J.,Liu, J. (deposition date: 2021-12-26, release date: 2022-10-26, Last modification date: 2023-11-29)

Primary citation

Zhang, Y.,Chen, R.,Dong, Y.,Zhu, J.,Su, K.,Liu, J.,Xu, J.
Structural Studies Reveal Unique Non-canonical Regulators of G Protein Signaling Homology (RH) Domains in Sorting Nexins.
J.Mol.Biol., 434:167823-167823, 2022

PubMed Abstract: As a subgroup of sorting nexins (SNXs) that contain regulator of G protein signaling homology (RH) domain, SNX-RH proteins, including SNX13, SNX14 and SNX25, were proposed to play bifunctional roles in protein sorting and GPCR signaling regulation. However, mechanistic details of SNX-RH proteins functioning via RH domain remain to be illustrated. Here, we delineate crystal structures of the RH domains of SNX13 and SNX25, revealing a homodimer of SNX13 RH domain mediated by unique extended α4 and α5 helices, and a thiol modulated homodimer of SNX25-RH triggered by a unique cysteine on α6 helix. Further studies showed that RH domains of SNX-RH do not possess binding capacity toward Gα subunits, owing to the lack of critical residues for interaction. Thus, this study identifies a group of novel non-canonical RH domains that can act as a dimerization module in sorting nexins, which provides structural basis for mechanism studies on SNX-RH protein functions.

PubMed: 36103920
DOI: 10.1016/j.jmb.2022.167823

Experimental method

X-RAY DIFFRACTION (1.35 Å)