9J22
structure of human urea transport protein slc14A1 with urea
Summary for 9J22
| Entry DOI | 10.2210/pdb9j22/pdb |
| EMDB information | 61086 |
| Descriptor | Urea transporter 1, UREA, PALMITIC ACID (3 entities in total) |
| Functional Keywords | human urea transport protein slc14a1, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 3 |
| Total formula weight | 131676.35 |
| Authors | |
| Primary citation | Lu, D.,Zhang, K.,Cheng, C.,Wu, D.,Yin, L.,Luo, Q.,Shi, M.,Ma, H.,Lu, X. Structural basis of the bifunctionality of Marinobacter salinexigens ZYF650 T glucosylglycerol phosphorylase in glucosylglycerol catabolism. J.Biol.Chem., 301:108127-108127, 2025 Cited by PubMed Abstract: 2-O-α-Glucosylglycerol (GG) is a natural heteroside synthesized by many cyanobacteria and a few heterotrophic bacteria under salt stress conditions. Bacteria produce GG in response to stimuli and degrade it once the stimulus diminishes. Heterotrophic bacteria utilize GG phosphorylase (GGP), a member of the GH13_18 family, via a two-step process consisting of phosphorolysis and hydrolysis for GG catabolism. However, the precise mechanism by which GGP degrades GG remains elusive. We determined the 3D structure of a recently identified GGP (MsGGP) of the deep-sea bacterium Marinobacter salinexigens ZYF650, in complex with glucose and glycerol, α-d-glucose-1-phosphate (αGlc1-P), and orthophosphate (inorganic phosphate) at resolutions of 2.5, 2.7, and 2.7 Å, respectively. Notably, the first αGlc1-P complex structure in the GH13_18 family, the complex of MsGGP and αGlc1-P, validates that GGP catalyzes GG decomposition through consecutive phosphorolysis and hydrolysis. In addition, the structure reveals the mechanism of high stereoselectivity on αGlc1-P. Glu231 and Asp190 were identified as the catalytic residues. Interestingly, these structures closely resemble each other, indicating minimal conformational changes upon binding end-product glucose and glycerol, or the intermediate αGlc1-P. The structures also indicate that the substrates may follow a specific trajectory and a precise order toward the active center in close proximity and in a geometrically favorable orientation for catalysis in a double displacement mechanism. PubMed: 39725037DOI: 10.1016/j.jbc.2024.108127 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.75 Å) |
Structure validation
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