In:
FEBS Letters, Wiley, Vol. 181, No. 1 ( 1985-02-11), p. 129-132
Abstract:
At pH 4.0, the RNase T 1 ‐2'GMP complex (1) crystallizes isomorphously with the isoenzyme complex (2) (Heinemann, U. and Saenger, W., 1982, Nature 299, 27‐31). The X‐ray structure of 1 was refined with 1.9 Å data to R = 0.195. Polypeptide folding is similar in 1 and 2. However, the sugar pucker of 2'‐GMP is 2'‐ endo (3' endo in 2), and guanine binding involves four hydrogen bonds in 1, which all differ from the two bonds in 2. Phosphate contacts Glu58, Arg77, Tyr38 in 1, but His40 in 2. These changes are not due to differences in sequence between the mother‐ and isoenzyme (Gln25‐Lys) but are associated with pH changes leadingto an inactive enzyme structure.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1016/0014-5793(85)81127-3
Language:
English
Publisher:
Wiley
Publication Date:
1985
detail.hit.zdb_id:
1460391-3
SSG:
12
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