| Autor: |
Willingham, Katrina, Maher, Megan J., Grunden, Amy M., Ghosh, Mousumi, Adams, Michael W. W., Freeman, Hans C., Gussa, J. Mitchell |
| Předmět: |
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| Zdroj: |
Acta Crystallographica: Section D (Wiley-Blackwell); Mar2001, Vol. 57 Issue 3, p428-430, 3p |
| Abstrakt: |
The prolidase (proline-specific amino dipeptidase) from the hyperthermophilic arch aeon Pyrococcus furiosus has been crystallized. The enzyme has been shown to be a homodimer and to require two Co atoms per subunit for optimum activity. Two crystal forms have been obtained under similar growth conditions. Both are monoclinic, space group P21. Form I has unit-cell parameters a = 130.4, b = 97.4, c = 129.9 Å, β = 118.3°. Form II has a smaller unit cell, with a = 56.5, b = 97.3, c = 70.0 Å, β = 97.1°. If the crystal density is assumed to lie near the center of the normal range then the form I crystals will have four dimers per asymmetric unit, whereas the form II crystals will have only one dimer in each asymmetric unit. Diffraction data have been recorded from native form I and form II crystals to resolutions of 3.2 and 1.95 Å, respectively. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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