Martha L. Ludwig

Affiliations: 
University of Michigan, Ann Arbor, Ann Arbor, MI 
Area:
structural biology
Website:
http://www.nasonline.org/publications/biographical-memoirs/memoir-pdfs/ludwig_martha.pdf
Google:
"Martha L. Ludwig"
Bio:

(1931 - 2006)
http://www.nasonline.org/member-directory/deceased-members/64326.html
http://dx.doi.org/10.1073/pnas.0401014101

Mean distance: 7.28
 
SNBCP
Cross-listing: MichiganTree

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Publications

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Datta S, Koutmos M, Pattridge KA, et al. (2008) A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor. Proceedings of the National Academy of Sciences of the United States of America. 105: 4115-20
Koutmos M, Pejchal R, Bomer TM, et al. (2008) Metal active site elasticity linked to activation of homocysteine in methionine synthases. Proceedings of the National Academy of Sciences of the United States of America. 105: 3286-91
Huang S, Romanchuk G, Pattridge K, et al. (2007) Reactivation of methionine synthase from Thermotoga maritima (TM0268) requires the downstream gene product TM0269. Protein Science : a Publication of the Protein Society. 16: 1588-95
Pejchal R, Campbell E, Guenther BD, et al. (2006) Structural perturbations in the Ala --> Val polymorphism of methylenetetrahydrofolate reductase: how binding of folates may protect against inactivation. Biochemistry. 45: 4808-18
Pejchal R, Sargeant R, Ludwig ML. (2005) Structures of NADH and CH3-H4folate complexes of Escherichia coli methylenetetrahydrofolate reductase reveal a spartan strategy for a ping-pong reaction. Biochemistry. 44: 11447-57
Pejchal R, Ludwig ML. (2005) Cobalamin-independent methionine synthase (MetE): a face-to-face double barrel that evolved by gene duplication. Plos Biology. 3: e31
Castro C, Gratson AA, Evans JC, et al. (2004) Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis. Biochemistry. 43: 5341-51
Evans JC, Huddler DP, Hilgers MT, et al. (2004) Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 101: 3729-36
Pattridge KA, Weber CH, Friesen JA, et al. (2003) Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis. The Journal of Biological Chemistry. 278: 51863-71
Bandarian V, Ludwig ML, Matthews RG. (2003) Factors modulating conformational equilibria in large modular proteins: a case study with cobalamin-dependent methionine synthase. Proceedings of the National Academy of Sciences of the United States of America. 100: 8156-63
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