5KO9
Crystal Structure of the SRAP Domain of Human HMCES Protein
Summary for 5KO9
| Entry DOI | 10.2210/pdb5ko9/pdb |
| Descriptor | Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein, UNKNOWN ATOM OR ION (3 entities in total) |
| Functional Keywords | srap domain, dna-binding, structural genomics, structural genomics consortium, sgc, dna binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 31802.82 |
| Authors | Halabelian, L.,Li, Y.,Bountra, C.,Edwards, A.M.,Arrowsmith, C.H.,Structural Genomics Consortium (SGC) (deposition date: 2016-06-29, release date: 2016-08-24, Last modification date: 2023-10-04) |
| Primary citation | Halabelian, L.,Ravichandran, M.,Li, Y.,Zeng, H.,Rao, A.,Aravind, L.,Arrowsmith, C.H. Structural basis of HMCES interactions with abasic DNA and multivalent substrate recognition. Nat.Struct.Mol.Biol., 26:607-612, 2019 Cited by PubMed Abstract: Embryonic stem cell-specific 5-hydroxymethylcytosine-binding protein (HMCES) can covalently cross-link to abasic sites in single-stranded DNA at stalled replication forks to prevent genome instability. Here, we report crystal structures of the human HMCES SOS response-associated peptidase (SRAP) domain in complex with DNA-damage substrates, including HMCES cross-linked with an abasic site within a 3' overhang DNA. HMCES interacts with both single-strand and duplex segments of DNA, with two independent duplex DNA interaction sites identified in the SRAP domain. The HMCES DNA-protein cross-link structure provides structural insights into a novel thiazolidine covalent interaction between the DNA abasic site and conserved Cys 2 of HMCES. Collectively, our structures demonstrate the capacity for the SRAP domain to interact with a variety of single-strand- and double-strand-containing DNA structures found in DNA-damage sites, including 5' and 3' overhang DNAs and gapped DNAs with short single-strand segments. PubMed: 31235913DOI: 10.1038/s41594-019-0246-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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