2WIU
Mercury-modified bacterial persistence regulator hipBA
Summary for 2WIU
| Entry DOI | 10.2210/pdb2wiu/pdb |
| Related | 3DNT 3DNU 3DNV 3DNW |
| Descriptor | PROTEIN HIPA, HTH-TYPE TRANSCRIPTIONAL REGULATOR HIPB, MERCURY (II) ION, ... (5 entities in total) |
| Functional Keywords | transferase transcription complex, serine kinase, dna-binding, mercury derivative, repressor, transcription regulation, sad, transferase-transcription complex, transferase/transcription |
| Biological source | ESCHERICHIA COLI More |
| Total number of polymer chains | 4 |
| Total formula weight | 122140.38 |
| Authors | Evdokimov, A.,Voznesensky, I.,Fennell, K.,Anderson, M.,Smith, J.F.,Fisher, D.A. (deposition date: 2009-05-17, release date: 2009-07-28, Last modification date: 2024-05-08) |
| Primary citation | Evdokimov, A.,Voznesensky, I.,Fennell, K.,Anderson, M.,Smith, J.F.,Fisher, D.A. New Kinase Regulation Mechanism Found in Hipba: A Bacterial Persistence Switch. Acta Crystallogr.,Sect.D, 65:875-, 2009 Cited by PubMed Abstract: Bacterial persistence is the ability of individual cells to randomly enter a period of dormancy during which the cells are protected against antibiotics. In Escherichia coli, persistence is regulated by the activity of a protein kinase HipA and its DNA-binding partner HipB, which is a strong inhibitor of both HipA activity and hip operon transcription. The crystal structure of the HipBA complex was solved by application of the SAD technique to a mercury derivative. In this article, the fortuitous and interesting effect of mercury soaks on the native HipBA crystals is discussed as well as the intriguing tryptophan-binding pocket found on the HipA surface. A HipA-regulation model is also proposed that is consistent with the available structural and biochemical data. PubMed: 19622872DOI: 10.1107/S0907444909018800 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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