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1lt7

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[[Image:1lt7.jpg|left|200px]]
 
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{{Structure
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==Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions==
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|PDB= 1lt7 |SIZE=350|CAPTION= <scene name='initialview01'>1lt7</scene>, resolution 2.15&Aring;
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<StructureSection load='1lt7' size='340' side='right'caption='[[1lt7]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene> and <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene>
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<table><tr><td colspan='2'>[[1lt7]] 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=1LT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LT7 FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5]
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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]] 2.15&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene></td></tr>
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}}
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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=1lt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt7 OCA], [https://pdbe.org/1lt7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lt7 RCSB], [https://www.ebi.ac.uk/pdbsum/1lt7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lt7 ProSAT]</span></td></tr>
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</table>
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'''Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions'''
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== Function ==
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[https://www.uniprot.org/uniprot/BHMT1_HUMAN BHMT1_HUMAN] Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Betaine-homocysteine methyl transferase (BHMT) catalyzes the synthesis of methionine from betaine and homocysteine (Hcy), utilizing a zinc ion to activate Hcy. BHMT is a key liver enzyme that is important for homocysteine homeostasis. X-ray structures of human BHMT in its oxidized (Zn-free) and reduced (Zn-replete) forms, the latter in complex with the bisubstrate analog, S(delta-carboxybutyl)-L-homocysteine, were determined at resolutions of 2.15 A and 2.05 A. BHMT is a (beta/alpha)(8) barrel that is distorted to construct the substrate and metal binding sites. The zinc binding sequences G-V/L-N-C and G-G-C-C are at the C termini of strands beta6 and beta8. Oxidation to the Cys217-Cys299 disulfide and expulsion of Zn are accompanied by local rearrangements. The structures identify Hcy binding fingerprints and provide a prototype for the homocysteine S-methyltransferase family.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/1lt7_consurf.spt"</scriptWhenChecked>
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1LT7 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=1LT7 OCA].
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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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==Reference==
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</jmolCheckbox>
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Betaine-homocysteine methyltransferase: zinc in a distorted barrel., Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML, Structure. 2002 Sep;10(9):1159-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12220488 12220488]
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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=1lt7 ConSurf].
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[[Category: Betaine--homocysteine S-methyltransferase]]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Castro, C.]]
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[[Category: Castro C]]
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[[Category: Evans, J C.]]
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[[Category: Evans JC]]
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[[Category: Garrow, T A.]]
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[[Category: Garrow TA]]
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[[Category: Huddler, D P.]]
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[[Category: Huddler DP]]
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[[Category: Jiracek, J.]]
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[[Category: Jiracek J]]
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[[Category: Ludwig, M L.]]
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[[Category: Ludwig ML]]
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[[Category: Millian, N S.]]
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[[Category: Millian NS]]
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[[Category: CIT]]
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[[Category: SM]]
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[[Category: homocysteine metabolism]]
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[[Category: homocysteinemia]]
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[[Category: thiol alkyl transfer]]
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[[Category: transferase]]
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[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:34:55 2008''
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Current revision

Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions

PDB ID 1lt7

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