1G3K
CRYSTAL STRUCTURE OF THE H. INFLUENZAE PROTEASE HSLV AT 1.9 A RESOLUTION
Summary for 1G3K
| Entry DOI | 10.2210/pdb1g3k/pdb |
| Related | 1G3I 1G41 |
| Descriptor | ATP-DEPENDENT PROTEASE HSLV, SODIUM ION (3 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Haemophilus influenzae |
| Cellular location | Cytoplasm (By similarity): P43772 |
| Total number of polymer chains | 3 |
| Total formula weight | 56779.62 |
| Authors | Sousa, M.C.,McKay, D.B. (deposition date: 2000-10-24, release date: 2000-11-22, Last modification date: 2024-04-03) |
| Primary citation | Sousa, M.C.,Trame, C.B.,Tsuruta, H.,Wilbanks, S.M.,Reddy, V.S.,McKay, D.B. Crystal and solution structures of an HslUV protease-chaperone complex. Cell(Cambridge,Mass.), 103:633-643, 2000 Cited by PubMed Abstract: HslUV is a "prokaryotic proteasome" composed of the HslV protease and the HslU ATPase, a chaperone of the Clp/Hsp100 family. The 3.4 A crystal structure of an HslUV complex is presented here. Two hexameric ATP binding rings of HslU bind intimately to opposite sides of the HslV protease; the HslU "intermediate domains" extend outward from the complex. The solution structure of HslUV, derived from small angle X-ray scattering data under conditions where the complex is assembled and active, agrees with this crystallographic structure. When the complex forms, the carboxy-terminal helices of HslU distend and bind between subunits of HslV, and the apical helices of HslV shift substantially, transmitting a conformational change to the active site region of the protease. PubMed: 11106733DOI: 10.1016/S0092-8674(00)00166-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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