1x19

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[[Image:1x19.gif|left|200px]]
 
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{{Structure
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==Crystal structure of BchU involved in bacteriochlorophyll c biosynthesis==
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|PDB= 1x19 |SIZE=350|CAPTION= <scene name='initialview01'>1x19</scene>, resolution 2.27&Aring;
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<StructureSection load='1x19' size='340' side='right'caption='[[1x19]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1x19]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlorobaculum_tepidum_TLS Chlorobaculum tepidum TLS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1X19 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.27&#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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=1x19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x19 OCA], [https://pdbe.org/1x19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1x19 RCSB], [https://www.ebi.ac.uk/pdbsum/1x19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1x19 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1x1a|1X1A]], [[1x1b|1X1B]], [[1x1c|1X1C]], [[1x1d|1X1D]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1x19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1x19 OCA], [http://www.ebi.ac.uk/pdbsum/1x19 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1x19 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/BCHU_CHLTE BCHU_CHLTE] Involved in the biosynthesis of the major light-harvesting pigment bacteriochlorophyll c (BChlc), which confers a significant competitive advantage to green sulfur bacteria living at limiting red and near-infrared light intensities (PubMed:15090495). Catalyzes the methylation at the C-20 position of the cyclic tetrapyrrole chlorin of bacteriochlorophyll d (BChld) to produce bacteriochlorophyll c (BChlc) using S-adenosylmethionine (SAM) as a methyl source (PubMed:15090495, PubMed:16797589).<ref>PMID:15090495</ref> <ref>PMID:16797589</ref>
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== Evolutionary Conservation ==
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'''Crystal structure of BchU involved in bacteriochlorophyll c biosynthesis'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x1/1x19_consurf.spt"</scriptWhenChecked>
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BchU plays a role in bacteriochlorophyll c biosynthesis by catalyzing methylation at the C-20 position of cyclic tetrapyrrole chlorin using S-adenosylmethionine (SAM) as a methyl source. This methylation causes red-shifts of the electronic absorption spectrum of the light-harvesting pigment, allowing green photosynthetic bacteria to adapt to low-light environments. We have determined the crystal structures of BchU and its complex with S-adenosylhomocysteine (SAH). BchU forms a dimer and each subunit consists of two domains, an N-terminal domain and a C-terminal domain. Dimerization occurs through interactions between the N-terminal domains and the residues responsible for the catalytic reaction are in the C-terminal domain. The binding site of SAH is located in a large cavity between the two domains, where SAH is specifically recognized by many hydrogen bonds and a salt-bridge. The electron density map of BchU in complex with an analog of bacteriochlorophyll c located its central metal near the SAH-binding site, but the tetrapyrrole ring was invisible, suggesting that binding of the ring to BchU is loose and/or occupancy of the ring is low. It is likely that His290 acts as a ligand for the central metal of the substrate. The orientation of the substrate was predicted by simulation, and allows us to propose a mechanism for the BchU directed methylation: the strictly conserved Tyr246 residue acts catalytically in the direct transfer of the methyl group from SAM to the substrate through an S(N)2-like mechanism.
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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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==About this Structure==
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</jmolCheckbox>
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1X19 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chlorobaculum_tepidum Chlorobaculum tepidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1X19 OCA].
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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=1x19 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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== References ==
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Crystal structures of BchU, a methyltransferase involved in bacteriochlorophyll c biosynthesis, and its complex with S-adenosylhomocysteine: implications for reaction mechanism., Wada K, Yamaguchi H, Harada J, Niimi K, Osumi S, Saga Y, Oh-Oka H, Tamiaki H, Fukuyama K, J Mol Biol. 2006 Jul 21;360(4):839-49. Epub 2006 Jun 8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16797589 16797589]
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<references/>
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[[Category: Chlorobaculum tepidum]]
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__TOC__
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[[Category: Single protein]]
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</StructureSection>
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[[Category: Fukuyama, K.]]
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[[Category: Chlorobaculum tepidum TLS]]
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[[Category: Wada, K.]]
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[[Category: Large Structures]]
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[[Category: Yamaguchi, H.]]
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[[Category: Fukuyama K]]
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[[Category: ado-hcy]]
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[[Category: Wada K]]
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[[Category: ado-met]]
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[[Category: Yamaguchi H]]
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[[Category: bacteriochllochlorophyll]]
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[[Category: bchu]]
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[[Category: methyltransferase]]
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[[Category: s-adenosylhomocysteine]]
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[[Category: s-adenosylmethyonine]]
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[[Category: sah]]
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[[Category: sam]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:43:32 2008''
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Current revision

Crystal structure of BchU involved in bacteriochlorophyll c biosynthesis

PDB ID 1x19

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