3Q4W
The structure of archaeal inorganic pyrophosphatase in complex with substrate
Summary for 3Q4W
| Entry DOI | 10.2210/pdb3q4w/pdb |
| Related | 3I98 3Q3L 3Q46 3Q5V 3Q9M |
| Descriptor | Tt-IPPase, CALCIUM ION, PYROPHOSPHATE 2-, ... (6 entities in total) |
| Functional Keywords | inorganic pyrophosphatase, hydrolase |
| Biological source | Thermococcus thioreducens |
| Total number of polymer chains | 1 |
| Total formula weight | 21279.97 |
| Authors | Hughes, R.C.,Meehan, E.J.,Coates, L.,Ng, J.D. (deposition date: 2010-12-24, release date: 2012-01-04, Last modification date: 2023-09-13) |
| Primary citation | Hughes, R.C.,Coates, L.,Blakeley, M.P.,Tomanicek, S.J.,Langan, P.,Kovalevsky, A.Y.,Garcia-Ruiz, J.M.,Ng, J.D. Inorganic pyrophosphatase crystals from Thermococcus thioreducens for X-ray and neutron diffraction. Acta Crystallogr.,Sect.F, 68:1482-1487, 2012 Cited by PubMed Abstract: Inorganic pyrophosphatase (IPPase) from the archaeon Thermococcus thioreducens was cloned, overexpressed in Escherichia coli, purified and crystallized in restricted geometry, resulting in large crystal volumes exceeding 5 mm3. IPPase is thermally stable and is able to resist denaturation at temperatures above 348 K. Owing to the high temperature tolerance of the enzyme, the protein was amenable to room-temperature manipulation at the level of protein preparation, crystallization and X-ray and neutron diffraction analyses. A complete synchrotron X-ray diffraction data set to 1.85 Å resolution was collected at room temperature from a single crystal of IPPase (monoclinic space group C2, unit-cell parameters a=106.11, b=95.46, c=113.68 Å, α=γ=90.0, β=98.12°). As large-volume crystals of IPPase can be obtained, preliminary neutron diffraction tests were undertaken. Consequently, Laue diffraction images were obtained, with reflections observed to 2.1 Å resolution with I/σ(I) greater than 2.5. The preliminary crystallographic results reported here set in place future structure-function and mechanism studies of IPPase. PubMed: 23192028DOI: 10.1107/S1744309112032447 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION |
Structure validation
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