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Pyridoxal phosphate site in glycogen phosphorylase b: structure in native enzyme and in three derivatives with modified cofactors.

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 ...

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Publication status:
Published

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Publisher copy:
10.1021/bi00399a053

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
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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

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