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5YGU

Crystal structure of Escherichia coli (strain K12) mRNA Decapping Complex RppH-DapF

Summary for 5YGU
Entry DOI10.2210/pdb5ygu/pdb
DescriptorDiaminopimelate epimerase, RNA pyrophosphohydrolase, L(+)-TARTARIC ACID, ... (5 entities in total)
Functional Keywordsrpph-dapf, decapping, hydrolase, isomerase-hydrolase complex, isomerase/hydrolase
Biological sourceEscherichia coli (strain K12)
More
Total number of polymer chains2
Total formula weight51986.40
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 citationWang, 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: 29931175
DOI: 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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