Summary for 5YCQ
| Entry DOI | 10.2210/pdb5ycq/pdb |
| Descriptor | Heat shock protein HspQ (2 entities in total) |
| Functional Keywords | heat shock protein, dna binding protein |
| Biological source | Escherichia coli (strain 55989 / EAEC) |
| Cellular location | Cytoplasm : B7LE66 |
| Total number of polymer chains | 1 |
| Total formula weight | 11930.83 |
| Authors | Abe, Y.,Shioi, S.,Kita, S.,Nakata, H.,Maenaka, K.,Kohda, D.,Katayama, T.,Ueda, T. (deposition date: 2017-09-08, release date: 2018-04-11, Last modification date: 2024-10-16) |
| Primary citation | Abe, Y.,Shioi, S.,Kita, S.,Nakata, H.,Maenaka, K.,Kohda, D.,Katayama, T.,Ueda, T. X-ray crystal structure of Escherichia coli HspQ, a protein involved in the retardation of replication initiation FEBS Lett., 591:3805-3816, 2017 Cited by PubMed Abstract: The heat shock protein HspQ (YccV) of Escherichia coli has been proposed to participate in the retardation of replication initiation in cells with the dnaA508 allele. In this study, we have determined the 2.5-Å-resolution X-ray structure of the trimer of HspQ, which is also the first structure of a member of the YccV superfamily. The acidic character of the HspQ trimer suggests an interaction surface with basic proteins. From these results, we discuss the cellular function of HspQ, including its relationship with the DnaA508 protein. PubMed: 29083032DOI: 10.1002/1873-3468.12892 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.503 Å) |
Structure validation
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