5YGU
Crystal structure of Escherichia coli (strain K12) mRNA Decapping Complex RppH-DapF
Summary for 5YGU
Entry DOI | 10.2210/pdb5ygu/pdb |
Descriptor | Diaminopimelate epimerase, RNA pyrophosphohydrolase, L(+)-TARTARIC ACID, ... (5 entities in total) |
Functional Keywords | rpph-dapf, decapping, hydrolase, isomerase-hydrolase complex, isomerase/hydrolase |
Biological source | Escherichia coli (strain K12) More |
Total number of polymer chains | 2 |
Total formula weight | 51986.40 |
Authors | Wang, Q.,Guan, Z.Y.,Zhang, D.L.,Zou, T.T.,Yin, P. (deposition date: 2017-09-27, release date: 2018-06-06, Last modification date: 2023-11-22) |
Primary citation | Wang, Q.,Zhang, D.,Guan, Z.,Li, D.,Pei, K.,Liu, J.,Zou, T.,Yin, P. DapF stabilizes the substrate-favoring conformation of RppH to stimulate its RNA-pyrophosphohydrolase activity in Escherichia coli. Nucleic Acids Res., 46:6880-6892, 2018 Cited by PubMed: 29931175DOI: 10.1093/nar/gky528 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.298 Å) |
Structure validation
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