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B. Brooks, R. Bruccoleri, B. Olafson, D. States, S. Swaminathan, M. Karplus (1983)
CHARMM: A program for macromolecular energy, minimization, and dynamics calculationsJournal of Computational Chemistry, 4
Shankar Kumar, J. Rosenberg, D. Bouzida, R. Swendsen, P. Kollman (1992)
THE weighted histogram analysis method for free‐energy calculations on biomolecules. I. The methodJournal of Computational Chemistry, 13
Alexander MacKerell, D. Bashford, M. Bellott, R. Dunbrack, J. Evanseck, M. Field, S. Fischer, J. Gao, H. Guo, S. Ha, D. Joseph-McCarthy, L. Kuchnir, K. Kuczera, F. Lau, C. Mattos, S. Michnick, T. Ngo, D. Nguyen, B. Prodhom, W. Reiher, B. Roux, M. Schlenkrich, J. Smith, R. Stote, J. Straub, M. Watanabe, J. Wiórkiewicz-Kuczera, D. Yin, M. Karplus (1998)
All-atom empirical potential for molecular modeling and dynamics studies of proteins.The journal of physical chemistry. B, 102 18
S. Pares, C. Cohen-addad, L. Sieker, M. Neuburger, R. Douce (1995)
Refined structures at 2 and 2.2 A resolution of two forms of the H-protein, a lipoamide-containing protein of the glycine decarboxylase complex.Acta crystallographica. Section D, Biological crystallography, 51 Pt 6
G. Torrie, J. Valleau (1977)
Nonphysical sampling distributions in Monte Carlo free-energy estimation: Umbrella samplingJournal of Computational Physics, 23
Magali Faure, Jacques Bourguignon, Michel Neuburger, D. Macherel, Larry Sieker, Raymond Ober, Richard Kahn, Claudine Cohen-Addad, Roland Douce (2000)
Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system 2. Crystal structures of H- and L-proteins.European journal of biochemistry, 267 10
U. Essmann, L. Perera, M. Berkowitz, T. Darden, Hsing-Chou Lee, L. Pedersen (1995)
A smooth particle mesh Ewald methodJournal of Chemical Physics, 103
V. Gueguen, D. Macherel, M. Neuburger, Christine Pierre, M. Jaquinod, P. Gans, R. Douce, J. Bourguignon (1999)
Structural and Functional Characterization of H Protein Mutants of the Glycine Decarboxylase Complex*The Journal of Biological Chemistry, 274
O. Roche, K. Hinsen, M. Field (1999)
Theoretical study of the conformation of the H‐protein lipoamide arm as a function of its terminal groupProteins: Structure, 36
R. Douce, J. Bourguignon, D. Macherel, M. Neuburger (1994)
The glycine decarboxylase system in higher plant mitochondria: structure, function and biogenesis.Biochemical Society transactions, 22 1
Jacques Bourguignon, Michel Neuburger, Roland Douce (1988)
Resolution and characterization of the glycine-cleavage reaction in pea leaf mitochondria. Properties of the forward reaction catalysed by glycine decarboxylase and serine hydroxymethyltransferase.The Biochemical journal, 255 1
L. Guilhaudis, J. Simorre, M. Blackledge, M. Neuburger, J. Bourguignon, R. Douce, D. Marion, P. Gans (1999)
Investigation of the local structure and dynamics of the H subunit of the mitochondrial glycine decarboxylase using heteronuclear NMR spectroscopy.Biochemistry, 38 26
S Kuman, D Bouzida, RH Swendsen, P Kollman, JM Rosenberg (1992)
The weighted histogram analysis method for free energy on biomolecules. I. The method, 13
The lipoamide arm of the H protein plays a pivotal role in the catalytic cycle of the glycine decarboxylase complex (GDC) by being successively methylamine loaded (Hmet), reduced (Hred), and oxidized (Hox). In a previous study, we calculated free‐energy surfaces as a function of the lipoamide arm position of the three forms of the wild‐type protein and found close agreement with the available experimental data. Our simulations, together with crystallographic and NMR data, showed that the methylamine‐loaded arm is locked in a cavity by interaction with Ser12, Glu14, and Asp67. In this work, we investigate the behavior of the methylamine‐loaded form of a mutant H protein (HEA) where Glu14 has been replaced by Ala. We find that the arm can still be held in the cavity but that the energy barrier to release of the arm is halved from ∼40 kcal mol−1 for Hmet to ∼12 kcal mol−1 for HEA. To compensate for the loss of Glu14, the methylamine group shifts toward Ser66 in the mutant form. These results provide a structural basis for the equilibrium between the loaded and the unloaded forms of the arm observed by Gueguen et al. (Gueguen et al., J Biol Chem 1999;274:26344–26352) in HEA. Proteins 2001;45:237–240. © 2001 Wiley‐Liss, Inc.
Proteins: Structure Function and Bioinformatics – Wiley
Published: Jan 15, 2001
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