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6KBU

Crystal structure of yedK

Summary for 6KBU
Entry DOI10.2210/pdb6kbu/pdb
DescriptorSOS response-associated protein, GLYCEROL (3 entities in total)
Functional Keywordsdna repair. abasic site., dna binding protein
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight55544.41
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 (2.1 Å)
Structure validation

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數據於2024-11-13公開中

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