5wrd

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Crystal structure of LC3B in complex with FYCO1 LIR

Structural highlights

5wrd is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:GOL
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MLP3B_MOUSE Ubiquitin-like modifier involved in formation of autophagosomal vacuoles (autophagosomes). Plays a role in mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation. Promotes primary ciliogenesis by removing OFD1 from centriolar satellites via the autophagic pathway.[UniProtKB:Q9GZQ8]

Publication Abstract from PubMed

FYVE and coiled-coil domain-containing protein 1 (FYCO1), a multidomain autophagy adaptor protein, mediates microtubule plus-end-directed autophagosome transport by interacting with kinesin motor proteins and with the autophagosomal membrane components microtubule-associated protein 1 light chain 3 (LC3), Rab7 and phosphatidylinositol 3-phosphate (PI3P). To establish the structural basis for the recognition of FYCO1 by LC3, the crystal structure of mouse LC3B in complex with the FYCO1 LC3-interacting region (LIR) motif peptide was determined. Structural analysis showed that the flanking sequences N-terminal and C-terminal to the LIR core sequence of FYCO1, as well as the tetrapeptide core sequence, were specifically recognized by LC3B and contributed to the binding. Moreover, comparisons of related structures revealed a conserved mechanism of FYCO1 recognition by different LC3 isoforms among different species.

The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif.,Sakurai S, Tomita T, Shimizu T, Ohto U Acta Crystallogr F Struct Biol Commun. 2017 Mar 1;73(Pt 3):130-137. doi:, 10.1107/S2053230X17001911. Epub 2017 Feb 21. PMID:28291748[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
4 reviews cite this structure
Atg8-Family Proteins-Structural Features and Molecular Interactions in Autophagy and Beyond.
Wesch et al. (2020)
3 more
9 other articles
No citations found

See Also

References

  1. ↑ Sakurai S, Tomita T, Shimizu T, Ohto U. The crystal structure of mouse LC3B in complex with the FYCO1 LIR reveals the importance of the flanking region of the LIR motif. Acta Crystallogr F Struct Biol Commun. 2017 Mar 1;73(Pt 3):130-137. doi:, 10.1107/S2053230X17001911. Epub 2017 Feb 21. PMID:28291748 doi:http://dx.doi.org/10.1107/S2053230X17001911

Contents


PDB ID 5wrd

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OCA

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