7U5H
Cryo-EM Structure of DNPEP
Summary for 7U5H
| Entry DOI | 10.2210/pdb7u5h/pdb |
| EMDB information | 26350 |
| Descriptor | Aspartyl aminopeptidase, ZINC ION (2 entities in total) |
| Functional Keywords | dnpep, aminopeptidase, tetrahedral symmetry, peptide binding protein |
| Biological source | Bos taurus (cattle) |
| Total number of polymer chains | 12 |
| Total formula weight | 624288.07 |
| Authors | Morgan, C.E.,Yu, E.W.,Zhang, Z. (deposition date: 2022-03-02, release date: 2022-12-14, Last modification date: 2025-06-04) |
| Primary citation | Morgan, C.E.,Zhang, Z.,Miyagi, M.,Golczak, M.,Yu, E.W. Toward structural-omics of the bovine retinal pigment epithelium. Cell Rep, 41:111876-111876, 2022 Cited by PubMed Abstract: The use of an integrated systems biology approach to investigate tissues and organs has been thought to be impracticable in the field of structural biology, where the techniques mainly focus on determining the structure of a particular biomacromolecule of interest. Here, we report the use of cryoelectron microscopy (cryo-EM) to define the composition of a raw bovine retinal pigment epithelium (RPE) lysate. From this sample, we simultaneously identify and solve cryo-EM structures of seven different RPE enzymes whose functions affect neurotransmitter recycling, iron metabolism, gluconeogenesis, glycolysis, axonal development, and energy homeostasis. Interestingly, dysfunction of these important proteins has been directly linked to several neurodegenerative disorders, including Huntington's disease, amyotrophic lateral sclerosis (ALS), Parkinson's disease, Alzheimer's disease, and schizophrenia. Our work underscores the importance of cryo-EM in facilitating tissue and organ proteomics at the atomic level. PubMed: 36577381DOI: 10.1016/j.celrep.2022.111876 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.32 Å) |
Structure validation
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