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4XPU

The crystal structure of EndoV from E.coli

Summary for 4XPU
Entry DOI10.2210/pdb4xpu/pdb
DescriptorEndonuclease V (2 entities in total)
Functional Keywordsendonuclease v, inosine, dna repair, rna cleavage, hydrolase
Biological sourceEscherichia coli O45:K1 (strain S88 / ExPEC)
Cellular locationCytoplasm : B7MIY4
Total number of polymer chains2
Total formula weight47835.39
Authors
Xie, W.,Zhang, Z. (deposition date: 2015-01-18, release date: 2015-08-19, Last modification date: 2023-11-08)
Primary citationZhang, Z.,Jia, Q.,Zhou, C.,Xie, W.
Crystal structure of E. coli endonuclease V, an essential enzyme for deamination repair
Sci Rep, 5:12754-12754, 2015
Cited by
PubMed Abstract: Endonuclease V (EndoV) is a ubiquitous protein present in all three kingdoms of life, responsible for the specific cleavages at the second phosphodiester bond 3' to inosine. E. coli EndoV (EcEndoV) is the first member discovered in the EndoV family. It is a small protein with a compact gene organization, yet with a wide spectrum of substrate specificities. However, the structural basis of its substrate recognition is not well understood. In this study, we determined the 2.4 Å crystal structure of EcEndoV. The enzyme preserves the general 'RNase H-like motif' structure. Two subunits are almost fully resolved in the asymmetric unit, but they are not related by any 2-fold axes. Rather, they establish "head-to-shoulder" contacts with loose interactions between each other. Mutational studies show that mutations that disrupt the association mode of the two subunits also decrease the cleavage efficiencies of the enzyme. Further biochemical studies suggest that EcEndoV is able to bind to single-stranded, undamaged DNA substrates without sequence specificity, and forms two types of complexes in a metal-independent manner, which may explain the wide spectrum of substrate specificities of EcEndoV.
PubMed: 26244280
DOI: 10.1038/srep12754
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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건을2025-03-05부터공개중

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