5Y38

Crystal structure of C7orf59-HBXIP complex

Summary for 5Y38

• Entry DOI: 10.2210/pdb5y38/pdb
• Descriptor: Ragulator complex protein LAMTOR5, Ragulator complex protein LAMTOR4, SULFATE ION, ... (4 entities in total)
• Functional Keywords: ragulator, lamtor, hbxip, c7orf59, signaling protein
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm: O43504; Lysosome : Q0VGL1
• Total number of polymer chains: 2
• Total formula weight: 21923.72

Authors

Zhang, T.,Ding, J. (deposition date: 2017-07-28, release date: 2017-12-06, Last modification date: 2023-11-22)

Primary citation

Zhang, T.,Wang, R.,Wang, Z.,Wang, X.,Wang, F.,Ding, J.
Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1
Nat Commun, 8:1394-1394, 2017

PubMed Abstract: Amino acid-dependent activation of the mechanistic target of rapamycin complex 1 (mTORC1) is mediated by Rag GTPases, which are recruited to the lysosome by the Ragulator complex consisting of p18, MP1, p14, HBXIP and C7orf59; however, the molecular mechanism is elusive. Here, we report the crystal structure of Ragulator, in which p18 wraps around the MP1-p14 and C7orf59-HBXIP heterodimers and the interactions of p18 with MP1, C7orf59, and HBXIP are essential for the assembly of Ragulator. There are two binding sites for the Roadblock domains of Rag GTPases: helix α1 of p18 and the two helices side of MP1-p14. The interaction of Ragulator with Rag GTPases is required for their cellular co-localization and can be competitively inhibited by C17orf59. Collectively, our data indicate that Ragulator functions as a scaffold to recruit Rag GTPases to lysosomal membrane in mTORC1 signaling.

PubMed: 29123114
DOI: 10.1038/s41467-017-01567-4

Experimental method

X-RAY DIFFRACTION (2.8 Å)