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1nbh

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(New page: 200px<br /><applet load="1nbh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nbh, resolution 2.8&Aring;" /> '''Structure of glycine ...)
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[[Image:1nbh.gif|left|200px]]<br /><applet load="1nbh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nbh, resolution 2.8&Aring;" />
 
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'''Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate, GNMT:SAM:Ace'''<br />
 
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==Overview==
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==Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate, GNMT:SAM:Ace==
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Methyltransfer reactions are some of the most important reactions in, biological systems. Glycine N-methyltransferase (GNMT) catalyzes the, S-adenosyl-l-methionine- (SAM-) dependent methylation of glycine to form, sarcosine. Unlike most SAM-dependent methyltransferases, GNMT has a, relatively high value and is weakly inhibited by the product, S-adenosyl-l-homocysteine (SAH). The major role of GNMT is believed to be, the regulation of the cellular SAM/SAH ratio, which is thought to play a, key role in SAM-dependent methyltransfer reactions. Crystal structures of, GNMT complexed with SAM and acetate (a potent competitive inhibitor of, Gly) and the R175K mutated enzyme complexed with SAM were determined at, 2.8 and 3.0 A resolutions, respectively. With these crystal structures and, the previously determined structures of substrate-free enzyme, a catalytic, mechanism has been proposed. Structural changes occur in the transitions, from the substrate-free to the binary complex and from the binary to the, ternary complex. In the ternary complex stage, an alpha-helix in the, N-terminus undergoes a major conformational change. As a result, the bound, SAM is firmly connected to protein and a "Gly pocket" is created near the, bound SAM. The second substrate Gly binds to Arg175 and is brought into, the Gly pocket. Five hydrogen bonds connect the Gly in the proximity of, the bound SAM and orient the lone pair orbital on the amino nitrogen (N), of Gly toward the donor methyl group (C(E)) of SAM. Thermal motion of the, enzyme leads to a collision of the N and C(E) so that a S(N)2, methyltransfer reaction occurs. The proposed mechanism is supported by, mutagenesis studies.
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<StructureSection load='1nbh' size='340' side='right'caption='[[1nbh]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1nbh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NBH FirstGlance]. <br>
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1NBH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ACT and SAM as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NBH OCA].
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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]] 2.8&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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==Reference==
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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=1nbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbh OCA], [https://pdbe.org/1nbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nbh RCSB], [https://www.ebi.ac.uk/pdbsum/1nbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbh ProSAT]</span></td></tr>
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Catalytic mechanism of glycine N-methyltransferase., Takata Y, Huang Y, Komoto J, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F, Biochemistry. 2003 Jul 22;42(28):8394-402. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12859184 12859184]
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</table>
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[[Category: Glycine N-methyltransferase]]
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== Function ==
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[https://www.uniprot.org/uniprot/GNMT_RAT GNMT_RAT] 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.
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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/nb/1nbh_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=1nbh ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Takata Y]]
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[[Category: Takata, Y.]]
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[[Category: Takusagawa F]]
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[[Category: Takusagawa, F.]]
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[[Category: ACT]]
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[[Category: SAM]]
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[[Category: enzyme catalytic mechanism]]
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[[Category: glycine n-methyltransferase]]
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[[Category: methyltransferase]]
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[[Category: s-adenosylmethionine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:07:03 2007''
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Current revision

Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate, GNMT:SAM:Ace

PDB ID 1nbh

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