7rrm | pdb_00007rrm

Structure of the human TMED1 (p24gamma1) Golgi dynamics Domain

spinqualitylabelsall models 7rrm, resolution 1.72Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7rrm is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.72Å Ligands: ACT, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TMED1_HUMAN Potential role in vesicular protein trafficking, mainly in the early secretory pathway. May act as a cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and may be involved in vesicle coat formation at the cytoplasmic side. Publication Abstract from PubMed The transmembrane emp24 domain-containing (TMED) proteins, also called p24 proteins, are members of a family of sorting receptors present in all representatives of the Eukarya and abundantly present in all subcompartments of the early secretory pathway, namely the endoplasmic reticulum (ER), the Golgi, and the intermediate compartment. Although essential during the bidirectional transport between the ER and the Golgi, there is still a lack of information regarding the TMED's structure across different subfamilies. Besides, although the presence of a TMED homo-oligomerization was suggested previously based on crystallographic contacts observed for the isolated Golgi Dynamics (GOLD) domain, no further analyses of its presence in solution were done. Here, we describe the first high-resolution structure of a TMED1 GOLD representative and its biophysical characterization in solution. The crystal structure showed a dimer formation that is also present in solution in a salt-dependent manner, suggesting that the GOLD domain can form homodimers in solution even in the absence of the TMED1 coiled-coil region. A molecular dynamics description of the dimer stabilization, with a phylogenetic analysis of the residues important for the oligomerization and a model for the orientation towards the lipid membrane, are also presented. Structural and thermodynamic analyses of human TMED1 (p24gamma1) Golgi dynamics.,Mota DCAM, Cardoso IA, Mori RM, Batista MRB, Basso LGM, Nonato MC, Costa-Filho AJ, Mendes LFS Biochimie. 2021 Oct 9. pii: S0300-9084(21)00228-5. doi:, 10.1016/j.biochi.2021.10.002. PMID:34634369 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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