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Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.

Forouhar F, Hussain M, Farid R, Benach J, Abashidze M, Edstrom WC, Vorobiev SM, Xiao R, Acton TB, Fu Z, Kim JJ, Miziorko HM, Montelione GT, Hunt JF,
Journal of Biological Chemistry (2006) 281(11):7533-45 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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The enzyme 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) lyase catalyzes the terminal steps in ketone body generation and leucine degradation. ...
chemistry enzymology 
Crystallography, X-Ray Protein Structure, Tertiary Oxidative Stress Protein Conformation Catalytic Domain Models, Chemical Protein Folding Binding Sites Brucella melitensis Protein Structure, Secondary Amino Acid Sequence Sequence Homology, Amino Acid Cations Chromatography, Gel 2-Isopropylmalate Synthase Aspartic Acid Models, Molecular Bacillus subtilis Humans Molecular Sequence Data Carbon Lysine Stereoisomerism Kinetics Point Mutation Oxo-Acid-Lyases Protein Binding Catalysis Light Scattering, Radiation 
16330546  
10.1074/jbc.M507996200  
22 (Last update: 03/25/2017 11:44:59am)  
1YDN
1YDO  
structure  
multiple pdbids [1ydo,1ydn]