Structure of Selenomonas ruminantium lactate dehydrogenase I85R mutant

S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE

Biochemical, structural and dynamical characterizations of the lactate dehydrogenase from Selenomonas ruminantium provide information about an intermediate evolutionary step prior to complete allosteric regulation acquisition in the super family of lactate and malate dehydrogenases.

MNNRRKIVVIGASNVGSAVANKIADFQLATEVVLIDLNEDKAWGEAKDSSHATSCIYSTNIKFHLGDYEDCKDANIIVIT
AGPSRRPGETPDRLKLAGTNAKIMSSVMGEIVKRTKEAMIIMITNPLDVATYVVSTQFDYPRNLILGTGTMLETYRFRRI
LADKYQVDPKNINGYVLGEHGNAAFVAWSTTGCAGFPIDDLDEYFHRTEKLSHEAVEQELVQVAYDVINKKGFTNTGIAM
AACRFIKSVLYDEHTILPCSAVLEGEYGIKDVALSIPRMVCADGIMRSFEVHLTDDELEKMHKAAQSVRSALDGAGIK

MNNRRKIVVIGASNVGSAVANKIADFQLATEVVLIDLNEDKAWGEAKDSSHATS(CSD)IYSTNIKFHLGDYEDCKDANI
IVITAGPSRRPGETPDRLKLAGTNAKIMSSVMGEIVKRTKEAMIIMITNPLDVATYVVSTQFDYPRNLILGTGTMLETYR
FRRILADKYQVDPKNINGYVLGEHGNAAFVAWSTTGCAGFPIDDLDEYFHRTEKLSHEAVEQELVQVAYDVINKKGFTNT
GIAMAACRFIKSVLYDEHTILPCSAVLEGEYGIKDVALSIPRMV(OCS)ADGIMRSFEVHLTDDELEKMHKAAQSVRSAL
DGAGIK

0.1 M BisTris propane pH 7.5, 0.2 M NaNO3, 16 to 26 % PEG 3,350 (optimized from Molecular Dimensions PACT screen, condition 77).

Allosteric regulation; lactate dehydrogenase; mutant, OXIDOREDUCTASE

CIYSTNIKFHLGDYEDCKDANIIVITAGPSIRPGETPDRLKLAGTNAKIMSSVMGEIVKRTKEAMIIMITNPLDVATYVV
STQFDYPRNLILGTGTMLETYRFRRILADKYQVDPKNINGYVLGEHGNAAFVAWSTTGCAGFPIDDLDEYFHRTEKLSHE
AVEQELVQVAYDVINKKGFTNTGIAMAACRFIKSVLYDEHTILPCSAVLEGEYGIKDVALSIPRM