6JLE

Crystal structure of MORN4/Myo3a complex

Summary for 6JLE

• Entry DOI: 10.2210/pdb6jle/pdb
• Descriptor: MORN repeat-containing protein 4, Myosin-IIIa, GLYCEROL, ... (5 entities in total)
• Functional Keywords: protein binding, protein transport, motor protein
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 2
• Total formula weight: 22531.88

Authors

Li, J.,Liu, H.,Raval, M.H.,Wan, J.,Yengo, C.M.,Liu, W.,Zhang, M. (deposition date: 2019-03-05, release date: 2019-07-24, Last modification date: 2024-03-27)

Primary citation

Li, J.,Liu, H.,Raval, M.H.,Wan, J.,Yengo, C.M.,Liu, W.,Zhang, M.
Structure of the MORN4/Myo3a Tail Complex Reveals MORN Repeats as Protein Binding Modules.
Structure, 27:1366-, 2019

PubMed Abstract: Tandem repeats are basic building blocks for constructing proteins with diverse structures and functions. Compared with extensively studied α-helix-based tandem repeats such as ankyrin, tetratricopeptide, armadillo, and HEAT repeat proteins, relatively little is known about tandem repeat proteins formed by β hairpins. In this study, we discovered that the MORN repeats from MORN4 function as a protein binding module specifically recognizing a tail cargo binding region from Myo3a. The structure of the MORN4/Myo3a complex shows that MORN4 forms an extended single-layered β-sheet structure and uses a U-shaped groove to bind to the Myo3a tail with high affinity and specificity. Sequence and structural analyses further elucidated the unique sequence features for folding and target binding of MORN repeats. Our work establishes that the β-hairpin-based MORN repeats are protein-protein interaction modules.

PubMed: 31279628
DOI: 10.1016/j.str.2019.06.004

Experimental method

X-RAY DIFFRACTION (1.55 Å)