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Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase.
Protein Sci 1999; 8(6):1218-31PS

Abstract

The first crystal structure of an inorganic pyrophosphatase (S-PPase) from an archaebacterium, the thermophile Sulfolobus acidocaldarius, has been solved by molecular replacement and refined to an R-factor of 19.7% at 2.7 A. S-PPase is a D3 homohexameric protein with one Mg2+ per active site in a position similar to, but not identical with, the first activating metal in mesophilic pyrophosphatases (PPase). In mesophilic PPases, Asp65, Asp70, and Asp102 coordinate the Mg2+, while only Asp65 and Asp102 do in S-PPase, and the Mg2+ moves by 0.7 A. S-PPase may therefore be deactivated at low temperature by mispositioning a key metal ion. The monomer S-PPase structure is very similar to that of Thermus thermophilus (T-PPase) and Escherichia coli (E-PPase), root-mean-square deviations around 1 A/Calpha. But the hexamer structures of S- and T-PPase are more tightly packed and more similar to each other than they are to that of E-PPase, as shown by the increase in surface area buried upon oligomerization. In T-PPase, Arg116 creates an interlocking ionic network to both twofold and threefold related monomers; S-PPase has hydrophilic interactions to threefold related monomers absent in both E- and T-PPase. In addition, the thermostable PPases have about 7% more hydrogen bonds per monomer than E-PPase, and, especially in S-PPase, additional ionic interactions anchor the C-terminus to the rest of the protein. Thermostability in PPases is thus due to subtle improvements in both monomer and oligomer interactions.

Authors+Show Affiliations

Department of Biochemistry and Food Technology, University of Turku, Finland.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10386872

Citation

Leppänen, V M., et al. "Sulfolobus Acidocaldarius Inorganic Pyrophosphatase: Structure, Thermostability, and Effect of Metal Ion in an Archael Pyrophosphatase." Protein Science : a Publication of the Protein Society, vol. 8, no. 6, 1999, pp. 1218-31.
Leppänen VM, Nummelin H, Hansen T, et al. Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase. Protein Sci. 1999;8(6):1218-31.
Leppänen, V. M., Nummelin, H., Hansen, T., Lahti, R., Schäfer, G., & Goldman, A. (1999). Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase. Protein Science : a Publication of the Protein Society, 8(6), pp. 1218-31.
Leppänen VM, et al. Sulfolobus Acidocaldarius Inorganic Pyrophosphatase: Structure, Thermostability, and Effect of Metal Ion in an Archael Pyrophosphatase. Protein Sci. 1999;8(6):1218-31. PubMed PMID: 10386872.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase. AU - Leppänen,V M, AU - Nummelin,H, AU - Hansen,T, AU - Lahti,R, AU - Schäfer,G, AU - Goldman,A, PY - 1999/7/1/pubmed PY - 1999/7/1/medline PY - 1999/7/1/entrez SP - 1218 EP - 31 JF - Protein science : a publication of the Protein Society JO - Protein Sci. VL - 8 IS - 6 N2 - The first crystal structure of an inorganic pyrophosphatase (S-PPase) from an archaebacterium, the thermophile Sulfolobus acidocaldarius, has been solved by molecular replacement and refined to an R-factor of 19.7% at 2.7 A. S-PPase is a D3 homohexameric protein with one Mg2+ per active site in a position similar to, but not identical with, the first activating metal in mesophilic pyrophosphatases (PPase). In mesophilic PPases, Asp65, Asp70, and Asp102 coordinate the Mg2+, while only Asp65 and Asp102 do in S-PPase, and the Mg2+ moves by 0.7 A. S-PPase may therefore be deactivated at low temperature by mispositioning a key metal ion. The monomer S-PPase structure is very similar to that of Thermus thermophilus (T-PPase) and Escherichia coli (E-PPase), root-mean-square deviations around 1 A/Calpha. But the hexamer structures of S- and T-PPase are more tightly packed and more similar to each other than they are to that of E-PPase, as shown by the increase in surface area buried upon oligomerization. In T-PPase, Arg116 creates an interlocking ionic network to both twofold and threefold related monomers; S-PPase has hydrophilic interactions to threefold related monomers absent in both E- and T-PPase. In addition, the thermostable PPases have about 7% more hydrogen bonds per monomer than E-PPase, and, especially in S-PPase, additional ionic interactions anchor the C-terminus to the rest of the protein. Thermostability in PPases is thus due to subtle improvements in both monomer and oligomer interactions. SN - 0961-8368 UR - https://www.unboundmedicine.com/medline/citation/10386872/Sulfolobus_acidocaldarius_inorganic_pyrophosphatase:_structure_thermostability_and_effect_of_metal_ion_in_an_archael_pyrophosphatase_ L2 - https://doi.org/10.1110/ps.8.6.1218 DB - PRIME DP - Unbound Medicine ER -