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2AZT

Crystal structure of H176N mutant of human Glycine N-Methyltransferase

Summary for 2AZT
Entry DOI10.2210/pdb2azt/pdb
Related1R74
DescriptorGlycine N-methyltransferase, BETA-MERCAPTOETHANOL, CITRIC ACID, ... (5 entities in total)
Functional Keywordsglycine n-methyltransferase, transferase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm: Q14749
Total number of polymer chains2
Total formula weight66330.79
Authors
Luka, Z.,Pakhomova, S.,Luka, Y.,Newcomer, M.E.,Wagner, C. (deposition date: 2005-09-12, release date: 2006-09-26, Last modification date: 2023-08-23)
Primary citationLuka, Z.,Pakhomova, S.,Luka, Y.,Newcomer, M.E.,Wagner, C.
Destabilization of human glycine N-methyltransferase by H176N mutation.
Protein Sci., 16:1957-1964, 2007
Cited by
PubMed Abstract: In the presence of moderate (2-4 M) urea concentrations the tetrameric enzyme, glycine N-methyltransferase (GNMT), dissociates into compact monomers. Higher concentrations of urea (7-8 M) promote complete denaturation of the enzyme. We report here that the H176N mutation in this enzyme, found in humans with hypermethioninaemia, significantly decreases stability of the tetramer, although H176 is located far from the intersubunit contact areas. Dissociation of the tetramer to compact monomers and unfolding of compact monomers of the mutant protein were detected by circular dichroism, quenching of fluorescence emission, size-exclusion chromatography, and enzyme activity. The values of apparent free energy of dissociation of tetramer and of unfolding of compact monomers for the H176N mutant (27.7 and 4.2 kcal/mol, respectively) are lower than those of wild-type protein (37.5 and 6.2 kcal/mol). A 2.7 A resolution structure of the mutant protein revealed no significant difference in the conformation of the protein near the mutated residue.
PubMed: 17660255
DOI: 10.1110/ps.072921507
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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数据于2025-10-15公开中

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