1r8x

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{{Seed}}
 
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[[Image:1r8x.png|left|200px]]
 
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==Crystal Structure of Mouse Glycine N-Methyltransferase (Tetragonal Form)==
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The line below this paragraph, containing "STRUCTURE_1r8x", creates the "Structure Box" on the page.
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<StructureSection load='1r8x' size='340' side='right'caption='[[1r8x]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1r8x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R8X FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
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<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=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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{{STRUCTURE_1r8x| PDB=1r8x | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1r8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r8x OCA], [https://pdbe.org/1r8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r8x RCSB], [https://www.ebi.ac.uk/pdbsum/1r8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r8x ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GNMT_MOUSE GNMT_MOUSE] 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 (By similarity).<ref>PMID:15340920</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/r8/1r8x_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1r8x ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Glycine N-methyltransferases (GNMTs) from three mammalian sources were compared with respect to their crystal structures and kinetic parameters. The crystal structure for the rat enzyme was published previously. Human and mouse GNMT were expressed in Escherichia coli in order to determine their crystal structures. Mouse GNMT was crystallized in two crystal forms, a monoclinic form and a tetragonal form. Comparison of the three structures reveals subtle differences, which may relate to the different kinetic properties of the enzymes.The flexible character of several loops surrounding the active site, along with an analysis of the active site boundaries, indicates that the observed conformations of human and mouse GNMTs are more open than that of the rat enzyme. There is an increase in kcat when going from rat to mouse to human, suggesting a correlation with the increased flexibility of some structural elements of the respective enzymes.
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===Crystal Structure of Mouse Glycine N-Methyltransferase (Tetragonal Form)===
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Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes.,Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME Proteins. 2004 Nov 1;57(2):331-7. PMID:15340920<ref>PMID:15340920</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15340920}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1r8x" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15340920 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15340920}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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1R8X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8X OCA].
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==Reference==
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Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes., Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME, Proteins. 2004 Nov 1;57(2):331-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15340920 15340920]
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Luka Z]]
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[[Category: Luka, Z.]]
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[[Category: Newcomer ME]]
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[[Category: Newcomer, M E.]]
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[[Category: Pakhomova S]]
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[[Category: Pakhomova, S.]]
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[[Category: Wagner C]]
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[[Category: Wagner, C.]]
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[[Category: Glycine n-methyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:12:29 2008''
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Current revision

Crystal Structure of Mouse Glycine N-Methyltransferase (Tetragonal Form)

PDB ID 1r8x

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