How coenzyme B12 radicals are generated: The crystal structure of methylmalonyl-coenzyme A mutase at 2 Å resolution

Structure

Volumn 4, Issue 3, 1996, Pages 339-350

  Mancia, Filippo ^a   Keep, Nicholas H ^a,b,f   Nakagawa, Atsushi ^a,g   Leadlay, Peter F ^b   McSweeney, Sean ^c,d   Rasmussen, Bjarne ^d   Bösecke, Peter ^e   Diat, Olivier ^e   Evans, Philip R ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^c DARESBURY LABORATORY   (United Kingdom)

^d EUROPEAN MOLECULAR BIOLOGY LABORATORY   (France)

^e EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

^f UNIVERSITY COLLEGE LONDON   (United Kingdom)

^g HOKKAIDO UNIVERSITY   (Japan)

Author keywords

Coenzyme B12; Methylmalonyl coenzyme A mutase; Radicals

Indexed keywords

COBAMAMIDE; FREE RADICAL; LIGAND; METHYLMALONYL COENZYME A MUTASE;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; ENZYME SPECIFICITY; ENZYMOLOGY; METABOLISM; PROPIONIBACTERIUM; PROTEIN SECONDARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

BINDING SITES; COBAMIDES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; FREE RADICALS; LIGANDS; METHYLMALONYL-COA MUTASE; MODELS, MOLECULAR; PROPIONIBACTERIUM; PROTEIN STRUCTURE, SECONDARY; SUBSTRATE SPECIFICITY;

PROPIONIBACTERIUM;

EID: 0030584657     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00037-8     Document Type: Article

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