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6KBZ

Crystal structure of yedK with ssDNA containing a tetrahydrofuran abasic site

Summary for 6KBZ
Entry DOI10.2210/pdb6kbz/pdb
DescriptorSOS response-associated protein, 5'-D (*CP*GP*GP*TP* (3DR) P*GP*AP*TP*TP*C)-3', MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsdna repair, abasic site, dna binding protein, dna binding protein-dna complex
Biological sourceEscherichia coli
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Total number of polymer chains8
Total formula weight114232.41
Authors
Wang, N.,Bao, H.,Huang, H. (deposition date: 2019-06-26, release date: 2019-07-10, Last modification date: 2023-11-22)
Primary citationWang, N.,Bao, H.,Chen, L.,Liu, Y.,Li, Y.,Wu, B.,Huang, H.
Molecular basis of abasic site sensing in single-stranded DNA by the SRAP domain of E. coli yedK.
Nucleic Acids Res., 47:10388-10399, 2019
Cited by
PubMed Abstract: HMCES and yedK were recently identified as sensors of abasic sites in ssDNA. In this study, we present multiple crystal structures captured in the apo-, nonspecific-substrate-binding, specific-substrate-binding, and product-binding states of yedK. In combination with biochemical data, we unveil the molecular basis of AP site sensing in ssDNA by yedK. Our results indicate that yedK has a strong preference for AP site-containing ssDNA over native ssDNA and that the conserved Glu105 residue is important for identifying AP sites in ssDNA. Moreover, our results reveal that a thiazolidine linkage is formed between yedK and AP sites in ssDNA, with the residues that stabilize the thiazolidine linkage important for the formation of DNA-protein crosslinks between yedK and the AP sites. We propose that our findings offer a unique platform to develop yedK and other SRAP domain-containing proteins as tools for detecting abasic sites in vitro and in vivo.
PubMed: 31504793
DOI: 10.1093/nar/gkz744
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.653 Å)
Structure validation

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