4uqu: Difference between revisions
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[[Category: Sulfurospirillum multivorans]] | [[Category: Sulfurospirillum multivorans]] | ||
[[Category: Tetrachloroethene reductive dehalogenase]] | [[Category: Tetrachloroethene reductive dehalogenase]] | ||
[[Category: Bommer, M | [[Category: Bommer, M]] | ||
[[Category: Diekert, G | [[Category: Diekert, G]] | ||
[[Category: Dobbek, H | [[Category: Dobbek, H]] | ||
[[Category: Fesseler, J | [[Category: Fesseler, J]] | ||
[[Category: Kunze, C | [[Category: Kunze, C]] | ||
[[Category: Schubert, T | [[Category: Schubert, T]] | ||
[[Category: Organohalide respiration]] | [[Category: Organohalide respiration]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] |
Revision as of 13:09, 25 January 2015
Crystal structure of the tetrachloroethene reductive dehalogenase from Sulfurospirillum multivoransCrystal structure of the tetrachloroethene reductive dehalogenase from Sulfurospirillum multivorans
Structural highlights
Publication Abstract from PubMedOrganohalide-respiring microorganisms can use a variety of persistent pollutants including trichloroethene (TCE) as terminal electron acceptors. The final two-electron transfer step in organohalide respiration is catalyzed by reductive dehalogenases. Here we report the x-ray crystal structure of PceA, an archetypal dehalogenase from Sulfurospirillum multivorans, as well as structures of PceA in complex with TCE and product analogs. The active site harbors a deeply buried norpseudo-B12 cofactor within a nitroreductase fold, also found in a mammalian B12 chaperone. The structures of PceA reveal how a cobalamin supports a reductive haloelimination exploiting a conserved B12-binding scaffold capped by a highly variable substrate-capturing region. Structural basis for organohalide respiration.,Bommer M, Kunze C, Fesseler J, Schubert T, Diekert G, Dobbek H Science. 2014 Oct 2. pii: 1258118. PMID:25278505[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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