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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1983 Sep;80(17):5289–5293. doi: 10.1073/pnas.80.17.5289

Crystal structures of the active site in specifically metal-depleted and cobalt-substituted horse liver alcohol dehydrogenase derivatives.

G Schneider, H Eklund, E Cedergren-Zeppezauer, M Zeppezauer
PMCID: PMC384239  PMID: 6351056

Abstract

Two derivatives of horse liver alcohol dehydrogenase (LADH) in which the active site is specifically metal-depleted [H4Zn(n)2LADH] or specifically Co-substituted [Co(c)2-Zn(n)2LADH] have been studied by crystallographic methods. (In these formulae, "n" identifies the noncatalytic zinc ion and "c" identifies the catalytic metal ion.) X-ray data were collected for H4Zn(n)2LADH to 2.7-A resolution and for Co(c)2Zn(n)2LADH to 2.4-A resolution. Difference Fourier maps demonstrate clearly that the catalytic zinc ions are removed in H4Zn(n)2LADH, whereas the noncatalytic zinc ions are still present. A 2.5-A shift in the sulphur position of cysteine-46 and a slight torsion of the imidazole ring of histidine-67 are the only changes in the protein structure that could be detected when compared to the native zinc enzyme. The structure of Co(c)2Zn(n)2LADH is essentially the same as that of the native enzyme. Each cobalt ion is bound to the ligands cysteine-46, cysteine-174, and histidine-67 and to a water molecule in a distorted tetrahedral geometry. A slight change in the position of histidine-67 was found. No further structural changes could be observed in the protein.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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