3GLA
Crystal Structure of the hspA from Xanthomonas axonopodis
Summary for 3GLA
| Entry DOI | 10.2210/pdb3gla/pdb |
| Related | 1GME 1SHS 2BOL |
| Descriptor | Low molecular weight heat shock protein, PHOSPHATE ION (3 entities in total) |
| Functional Keywords | hspa, shp, shsp, xanthomonas axonopodis, high resolution, stress response, chaperone |
| Biological source | Xanthomonas axonopodis pv. citri (Citrus canker) |
| Total number of polymer chains | 2 |
| Total formula weight | 22811.36 |
| Authors | Hilario, E.,Medrano, F.J.,Bertolini, M.C. (deposition date: 2009-03-11, release date: 2009-03-24, Last modification date: 2023-09-06) |
| Primary citation | Hilario, E.,Teixeira, E.C.,Pedroso, G.A.,Bertolini, M.C.,Medrano, F.J. Crystallization and preliminary X-ray diffraction analysis of XAC1151, a small heat-shock protein from Xanthomonas axonopodis pv. citri belonging to the alpha-crystallin family Acta Crystallogr.,Sect.F, 62:446-448, 2006 Cited by PubMed Abstract: The hspA gene (XAC1151) from Xanthomonas axonopodis pv. citri encodes a protein of 158 amino acids that belongs to the small heat-shock protein (sHSP) family of proteins. These proteins function as molecular chaperones by preventing protein aggregation. The protein was crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium phosphate. X-ray diffraction data were collected to 1.65 angstroms resolution using a synchrotron-radiation source. The crystal belongs to the rhombohedral space group R3, with unit-cell parameters a = b = 128.7, c = 55.3 angstroms. The crystal structure was solved by molecular-replacement methods. Structure refinement is in progress. PubMed: 16682772DOI: 10.1107/S174430910601219X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.64 Å) |
Structure validation
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