| Autor: |
Shimoni‐Livny, L., Carrell, H. L., Wagner, T., Kaufman Katz, A., Afshar, C., Mitchell, L. W., Volin, M., Jaffe, E. K., Glusker, J. P. |
| Zdroj: |
Acta Crystallographica Section D: Biological Crystallography; May 1998, Vol. 54 Issue: 3 p438-440, 3p |
| Abstrakt: |
Porphobilinogen synthase (PBGS) catalyzes the condensation of two identical substrate molecules, 5‐aminolevulinic acid (ALA), in an asymmetric manner to form porphobilinogen. E. coliPBGS is an homooctameric enzyme. The number of active sites is not clear, but each subunit binds one ZnIIion and one MgIIion. Diffraction‐quality crystals of native E. coliPBGS have been obtained, and unit‐cell dimensions (a130.8, c144.0 Å) are reported. These crystals diffract to about 3.0 Å resolution. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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