2azt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:31, 23 August 2023) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2azt.gif|left|200px]]
 
-
<!--
+
==Crystal structure of H176N mutant of human Glycine N-Methyltransferase==
-
The line below this paragraph, containing "STRUCTURE_2azt", creates the "Structure Box" on the page.
+
<StructureSection load='2azt' size='340' side='right'caption='[[2azt]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2azt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AZT FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
-
{{STRUCTURE_2azt| PDB=2azt | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2azt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2azt OCA], [https://pdbe.org/2azt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2azt RCSB], [https://www.ebi.ac.uk/pdbsum/2azt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2azt ProSAT]</span></td></tr>
-
 
+
</table>
-
'''Crystal structure of H176N mutant of human Glycine N-Methyltransferase'''
+
== Disease ==
-
 
+
[https://www.uniprot.org/uniprot/GNMT_HUMAN GNMT_HUMAN] Defects in GNMT are the cause of glycine N-methyltransferase deficiency (GNMT deficiency) [MIM:[https://omim.org/entry/606664 606664]; also known as hypermethioninemia. The only clinical abnormalities in patients with this deficiency are mild hepatomegaly and chronic elevation of serum transaminases.
-
 
+
== Function ==
-
==Overview==
+
[https://www.uniprot.org/uniprot/GNMT_HUMAN GNMT_HUMAN] Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine.<ref>PMID:15340920</ref> <ref>PMID:17660255</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/az/2azt_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2azt ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
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.
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==
+
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<ref>PMID:17660255</ref>
-
Known disease associated with this structure: Glycine N-methyltransferase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606628 606628]]
+
-
 
+
-
==About this Structure==
+
-
2AZT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AZT OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
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:[http://www.ncbi.nlm.nih.gov/pubmed/17660255 17660255]
+
</div>
-
[[Category: Glycine N-methyltransferase]]
+
<div class="pdbe-citations 2azt" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Luka, Y.]]
+
[[Category: Luka Y]]
-
[[Category: Luka, Z.]]
+
[[Category: Luka Z]]
-
[[Category: Newcomer, M E.]]
+
[[Category: Newcomer ME]]
-
[[Category: Pakhomova, S.]]
+
[[Category: Pakhomova S]]
-
[[Category: Wagner, C.]]
+
[[Category: Wagner C]]
-
[[Category: Glycine n-methyltransferase]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:40:24 2008''
+

Current revision

Crystal structure of H176N mutant of human Glycine N-Methyltransferase

PDB ID 2azt

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2azt"
Personal tools