4EPE
Final Urease Structure for Radiation Damage Experiment at 300 K
Summary for 4EPE
| Entry DOI | 10.2210/pdb4epe/pdb |
| Related | 4EP8 4EPB 4EPD |
| Descriptor | Urease subunit alpha, Urease subunit beta, Urease subunit gamma, ... (5 entities in total) |
| Functional Keywords | alpha-beta barrel, nickel metalloenzyme, hydrolase, radiation damage |
| Biological source | Enterobacter aerogenes More |
| Cellular location | Cytoplasm (By similarity): P18314 P18315 P18316 |
| Total number of polymer chains | 3 |
| Total formula weight | 82622.17 |
| Authors | Warkentin, M.,Badeau, R.,Hopkins, J.B.,Thorne, R.E. (deposition date: 2012-04-17, release date: 2012-08-29, Last modification date: 2013-01-23) |
| Primary citation | Warkentin, M.,Badeau, R.,Hopkins, J.B.,Thorne, R.E. Spatial distribution of radiation damage to crystalline proteins at 25-300 K. Acta Crystallogr.,Sect.D, 68:1108-1117, 2012 Cited by PubMed Abstract: The spatial distribution of radiation damage (assayed by increases in atomic B factors) to thaumatin and urease crystals at temperatures ranging from 25 to 300 K is reported. The nature of the damage changes dramatically at approximately 180 K. Above this temperature the role of solvent diffusion is apparent in thaumatin crystals, as solvent-exposed turns and loops are especially sensitive. In urease, a flap covering the active site is the most sensitive part of the molecule and nearby loops show enhanced sensitivity. Below 180 K sensitivity is correlated with poor local packing, especially in thaumatin. At all temperatures, the component of the damage that is spatially uniform within the unit cell accounts for more than half of the total increase in the atomic B factors and correlates with changes in mosaicity. This component may arise from lattice-level, rather than local, disorder. The effects of primary structure on radiation sensitivity are small compared with those of tertiary structure, local packing, solvent accessibility and crystal contacts. PubMed: 22948911DOI: 10.1107/S0907444912021361 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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