3q4w

The structure of archaeal inorganic pyrophosphatase in complex with substrate

spinqualitylabelsall models 3q4w, resolution 1.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q4w is a 1 chain structure with sequence from Atcc baa-394. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BR, CA, NA, POP Related: 3i98, 3q3l, 3q46, 3q5v, 3q9m Gene: Tt-IPPase (ATCC BAA-394) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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 A 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 A, alpha=gamma=90.0, beta=98.12 degrees ). 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 A resolution with I/sigma(I) greater than 2.5. The preliminary crystallographic results reported here set in place future structure-function and mechanism studies of IPPase. Inorganic pyrophosphatase crystals from Thermococcus thioreducens for X-ray and neutron diffraction.,Hughes RC, Coates L, Blakeley MP, Tomanicek SJ, Langan P, Kovalevsky AY, Garcia-Ruiz JM, Ng JD Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1482-7., doi: 10.1107/S1744309112032447. Epub 2012 Nov 14. PMID:23192028 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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