5GYK

Crystal Structure of Mdm12-deletion mutant

Summary for 5GYK

• Entry DOI: 10.2210/pdb5gyk/pdb
• Related: 5GYD
• Descriptor: Mitochondrial distribution and morphology protein 12, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine (2 entities in total)
• Functional Keywords: mdm12, ermes complex, smp domain, transport protein, lipid transport
• Biological source: Saccharomyces cerevisiae S288c (yeast); More
• Cellular location: Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side: Q92328
• Total number of polymer chains: 6
• Total formula weight: 160506.41

Authors

Jeong, H.,Park, J.,Lee, C. (deposition date: 2016-09-22, release date: 2016-11-16, Last modification date: 2023-11-08)

Primary citation

Jeong, H.,Park, J.,Lee, C.
Crystal structure of Mdm12 reveals the architecture and dynamic organization of the ERMES complex
EMBO Rep., 17:1857-1871, 2016

PubMed Abstract: The endoplasmic reticulum-mitochondria encounter structure (ERMES) is a protein complex that plays a tethering role in physically connecting ER and mitochondria membranes. The ERMES complex is composed of Mdm12, Mmm1, and Mdm34, which have a SMP domain in common, and Mdm10. Here, we report the crystal structure of S. cerevisiae Mdm12. The Mdm12 forms a dimeric SMP structure through domain swapping of the β1-strand comprising residues 1-7. Biochemical experiments reveal a phospholipid-binding site located along a hydrophobic channel of the Mdm12 structure and that Mdm12 might have a binding preference for glycerophospholipids harboring a positively charged head group. Strikingly, both full-length Mdm12 and Mdm12 truncated to exclude the disordered region (residues 74-114) display the same organization in the asymmetric unit, although they crystallize as a tetramer and hexamer, respectively. Taken together, these studies provide a novel understanding of the overall organization of SMP domains in the ERMES complex, indicating that Mdm12 interacts with Mdm34 through head-to-head contact, and with Mmm1 through tail-to-tail contact of SMP domains.

PubMed: 27821511
DOI: 10.15252/embr.201642706

Experimental method

X-RAY DIFFRACTION (3.596 Å)