 |
PDBsum entry 1hsd
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Oxidoreductase
|
PDB id
|
|
|
|
1hsd
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Three-Dimensional structure of holo 3 alpha,20 beta-Hydroxysteroid dehydrogenase: a member of a short-Chain dehydrogenase family.
|
|
|
Authors
|
|
D.Ghosh,
C.M.Weeks,
P.Grochulski,
W.L.Duax,
M.Erman,
R.L.Rimsay,
J.C.Orr.
|
|
|
Ref.
|
|
Proc Natl Acad Sci U S A, 1991,
88,
10064-10068.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The x-ray structure of a short-chain dehydrogenase, the bacterial holo 3
alpha,20 beta-hydroxysteroid dehydrogenase (EC 1.1.1.53), is described at 2.6 A
resolution. This enzyme is active as a tetramer and crystallizes with four
identical subunits in the asymmetric unit. It has the alpha/beta fold
characteristic of the dinucleotide binding region. The fold of the rest of the
subunit, the quaternary structure, and the nature of the cofactor-enzyme
interactions are, however, significantly different from those observed in the
long-chain dehydrogenases. The architecture of the postulated active site is
consistent with the observed stereospecificity of the enzyme and the fact that
the tetramer is the active form. There is only one cofactor and one
substrate-binding site per subunit; the specificity for both 3 alpha- and 20
beta-ends of the steroid results from the binding of the steroid in two
orientations near the same cofactor at the same catalytic site.
|
|
|
|
|
|
|
|
Headers
|
|
|
|
|
|
