Bibliographic Details
| Title: |
Structure of Escherichi coli uridine phosphorylase at 2.0 Å. |
| Authors: |
Burling, F. Temple, Kniewel, Ryan, Buglino, John A., Chadha, Tanya, Beckwith, Andrew, Lima, Christopher D. |
| Source: |
Acta Crystallographica: Section D (Wiley-Blackwell). Jan2003, Vol. 59 Issue 1, p73. 4p. |
| Subjects: |
Uridine, Molecular structure, Escherichia coli |
| Abstract: |
The 2.0 Å crystal structure has been determined for Escherichia coli uridine phosphorylase (UP), an essential enzyme in nucleotide biosynthesis that catalyzes the phosphorolytic cleavage of the C-N glycosidic bond of uridine to ribose-1-phosphate and uracil. The structure determination of two independent monomers in the asymmetric unit revealed the residue composition and atomic details of the apo configurations of each active site. The native hexameric UP enzyme was revealed by applying threefold crystallographic symmetry to the contents of the asymmetric unit. The 2.0 Å model reveals a closer structural relationship to other nucleotide phosphorylase enzymes than was previously appreciated. [ABSTRACT FROM AUTHOR] |
|
Copyright of Acta Crystallographica: Section D (Wiley-Blackwell) is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) |
| Database: |
Engineering Source |
