- Abstract:
-
The detailed environment of the essential cofactor pyridoxal 5'-phosphate in glycogen phosphorylase b, resulting from crystallographic refinement at 1.9-A resolution, is described. The pyridoxal ring is buried in a nonpolar site containing three aromatic rings while the 5'-phosphate group is highly solvated and makes only three direct contacts to the protein. The pyridine nitrogen interacts via a water with protein atoms [main chain carbonyl oxygen (Asn-133) and OH of tyrosine (Tyr-90)]. The ...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1021/bi00399a053
-
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- Journal:
- Biochemistry
- Volume:
- 26
- Issue:
- 25
- Pages:
- 8381-8389
- Publication date:
- 1987-12-05
- DOI:
- EISSN:
-
1520-4995
- ISSN:
-
0006-2960
- URN:
-
uuid:b5d239e7-b008-418e-bf24-936eeaca5167
- Source identifiers:
-
21095
- Local pid:
- pubs:21095
- Copyright date:
- 1987
Journal article
Pyridoxal phosphate site in glycogen phosphorylase b: structure in native enzyme and in three derivatives with modified cofactors.
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