1JMV
Structure of Haemophylus influenzae Universal Stress Protein At 1.85A Resolution
Summary for 1JMV
Entry DOI | 10.2210/pdb1jmv/pdb |
Descriptor | Universal Stress Protein A, SULFATE ION (3 entities in total) |
Functional Keywords | universal stress protein, uspa, chaperone |
Biological source | Haemophilus influenzae |
Cellular location | Cytoplasm (By similarity): P44880 |
Total number of polymer chains | 4 |
Total formula weight | 63488.38 |
Authors | Sousa, M.C.,McKay, D.B. (deposition date: 2001-07-20, release date: 2001-12-12, Last modification date: 2024-02-07) |
Primary citation | Sousa, M.C.,McKay, D.B. Structure of the universal stress protein of Haemophilus influenzae. Structure, 9:1135-1141, 2001 Cited by PubMed Abstract: The universal stress protein UspA is a small cytoplasmic bacterial protein whose expression is enhanced several-fold when cellular viability is challenged with heat shock, nutrient starvation, stress agents which arrest cell growth, or DNA-damaging agents. UspA enhances the rate of cell survival during prolonged exposure to such conditions, suggesting that it asserts a general "stress endurance" activity. However, neither the structure of UspA nor the biochemical mechanism by which it protects cells from the broad spectrum of stress agents is known. PubMed: 11738040DOI: 10.1016/S0969-2126(01)00680-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
Download full validation report
