4UR2

Crystal structure of the PCE reductive dehalogenase from S. multivorans in complex with iodide

Summary for 4UR2

• Entry DOI: 10.2210/pdb4ur2/pdb
• Related: 4UQU 4UR0 4UR1 4UR3
• Descriptor: TETRACHLOROETHENE REDUCTIVE DEHALOGENASE CATALYTIC SUBUNIT PCEA, IRON/SULFUR CLUSTER, NORPSEUDO-B12, ... (6 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: SULFUROSPIRILLUM MULTIVORANS
• Total number of polymer chains: 2
• Total formula weight: 110386.47

Authors

Bommer, M.,Kunze, C.,Fesseler, J.,Schubert, T.,Diekert, G.,Dobbek, H. (deposition date: 2014-06-25, release date: 2014-10-15, Last modification date: 2024-05-08)

Primary citation

Bommer, M.,Kunze, C.,Fesseler, J.,Schubert, T.,Diekert, G.,Dobbek, H.
Structural Basis for Organohalide Respiration.
Science, 346:455-, 2014

PubMed Abstract: Organohalide-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.

PubMed: 25278505
DOI: 10.1126/SCIENCE.1258118

Experimental method

X-RAY DIFFRACTION (2.096 Å)