6nua

DNA-protein crosslink between E. coli YedK and ssDNA containing an abasic site

spinqualitylabelsall models 6nua, resolution 1.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nua is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.64Å Ligands: PED Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function YEDK_ECOLI Publication Abstract from PubMed Abasic (AP) sites are one of the most common DNA lesions that block replicative polymerases. 5-hydroxymethylcytosine binding, embryonic stem cell-specific protein (HMCES) recognizes and processes these lesions in the context of single-stranded DNA (ssDNA). A HMCES DNA-protein cross-link (DPC) intermediate is thought to shield the AP site from endonucleases and error-prone polymerases. The highly evolutionarily conserved SOS-response associated peptidase (SRAP) domain of HMCES and its Escherichia coli ortholog YedK mediate lesion recognition. Here we uncover the basis of AP site protection by SRAP domains from a crystal structure of the YedK DPC. YedK forms a stable thiazolidine linkage between a ring-opened AP site and the alpha-amino and sulfhydryl substituents of its amino-terminal cysteine residue. The thiazolidine linkage explains the remarkable stability of the HMCES DPC, its resistance to strand cleavage and the proteolysis requirement for resolution. Furthermore, its structure reveals that HMCES has specificity for AP sites in ssDNA at junctions found when replicative polymerases encounter the AP lesion. Protection of abasic sites during DNA replication by a stable thiazolidine protein-DNA cross-link.,Thompson PS, Amidon KM, Mohni KN, Cortez D, Eichman BF Nat Struct Mol Biol. 2019 Jul;26(7):613-618. doi: 10.1038/s41594-019-0255-5. Epub, 2019 Jun 24. PMID:31235915 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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