2azt

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[[Image:2azt.gif|left|200px]]
[[Image:2azt.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2azt |SIZE=350|CAPTION= <scene name='initialview01'>2azt</scene>, resolution 2.70&Aring;
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The line below this paragraph, containing "STRUCTURE_2azt", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_N-methyltransferase Glycine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.20 2.1.1.20] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= GNMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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-->
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|DOMAIN=
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{{STRUCTURE_2azt| PDB=2azt | SCENE= }}
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|RELATEDENTRY=[[1r74|1R74]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2azt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2azt OCA], [http://www.ebi.ac.uk/pdbsum/2azt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2azt RCSB]</span>
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}}
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'''Crystal structure of H176N mutant of human Glycine N-Methyltransferase'''
'''Crystal structure of H176N mutant of human Glycine N-Methyltransferase'''
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[[Category: Pakhomova, S.]]
[[Category: Pakhomova, S.]]
[[Category: Wagner, C.]]
[[Category: Wagner, C.]]
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[[Category: glycine n-methyltransferase]]
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[[Category: Glycine n-methyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:40:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:59:31 2008''
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Revision as of 16:40, 3 May 2008

Image:2azt.gif

Template:STRUCTURE 2azt

Crystal structure of H176N mutant of human Glycine N-Methyltransferase


Contents

Overview

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.

Disease

Known disease associated with this structure: Glycine N-methyltransferase deficiency OMIM:[606628]

About this Structure

2AZT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Destabilization of human glycine N-methyltransferase by H176N mutation., Luka Z, Pakhomova S, Luka Y, Newcomer ME, Wagner C, Protein Sci. 2007 Sep;16(9):1957-64. Epub 2007 Jul 27. PMID:17660255 Page seeded by OCA on Sat May 3 19:40:24 2008

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OCA

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