1IM2
HslU, Haemophilus Influenzae, Selenomethionine Variant
Summary for 1IM2
| Entry DOI | 10.2210/pdb1im2/pdb |
| Related | 1DO0 1DO2 1G41 |
| Descriptor | ATP-DEPENDENT HSL PROTEASE ATP-BINDING SUBUNIT HSLU, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total) |
| Functional Keywords | chaperone, aaa family |
| Biological source | Haemophilus influenzae |
| Cellular location | Cytoplasm (By similarity): P43773 |
| Total number of polymer chains | 1 |
| Total formula weight | 50668.19 |
| Authors | Trame, C.B.,McKay, D.B. (deposition date: 2001-05-09, release date: 2001-08-08, Last modification date: 2024-10-30) |
| Primary citation | Trame, C.B.,McKay, D.B. Structure of Haemophilus influenzae HslU protein in crystals with one-dimensional disorder twinning. Acta Crystallogr.,Sect.D, 57:1079-1090, 2001 Cited by PubMed Abstract: The structure of the Haemophilus influenzae HslU protein, a molecular chaperone of the Clp/Hsp100 family, has been solved to 2.3 A by molecular replacement using a model of the homologous Escherichia coli protein. The crystals in which the structure was solved have an unusual twinning, or one-dimensional disorder, in which each successive crystal-packing layer is displaced laterally relative to the one below it. A model for the twinning and an algorithm for detwinning the data are described. It is known from other work that when the HslU hexamer binds its cognate protease HslV, the carboxy-terminal helices of HslU protomers distend and bind between HslV subunits. Comparison of HslU alone with its structure in the HslUV complex reveals several conserved amino-acid residues whose side-chain interactions differ between the two structures, suggesting that they may be part of a conformational switch that facilitates the release of the HslU carboxy-terminal helices when HslV binds. PubMed: 11468391DOI: 10.1107/S0907444901007673 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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