1x19

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1x19" size="450" color="white" frame="true" align="right" spinBox="true" caption="1x19, resolution 2.27&Aring;" /> '''Crystal structure of...)
Current revision (13:35, 13 March 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1x19.gif|left|200px]]<br /><applet load="1x19" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1x19, resolution 2.27&Aring;" />
 
-
'''Crystal structure of BchU involved in bacteriochlorophyll c biosynthesis'''<br />
 
-
==Overview==
+
==Crystal structure of BchU involved in bacteriochlorophyll c biosynthesis==
-
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.
+
<StructureSection load='1x19' size='340' side='right'caption='[[1x19]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<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>
-
1X19 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Chlorobaculum_tepidum Chlorobaculum tepidum] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1X19 OCA].
+
</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>
-
 
+
<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>
-
==Reference==
+
<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>
-
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16797589 16797589]
+
</table>
-
[[Category: Chlorobaculum tepidum]]
+
== Function ==
-
[[Category: Single protein]]
+
[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>
-
[[Category: Fukuyama, K.]]
+
== Evolutionary Conservation ==
-
[[Category: Wada, K.]]
+
[[Image:Consurf_key_small.gif|200px|right]]
-
[[Category: Yamaguchi, H.]]
+
Check<jmol>
-
[[Category: SO4]]
+
<jmolCheckbox>
-
[[Category: ado-hcy]]
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x1/1x19_consurf.spt"</scriptWhenChecked>
-
[[Category: ado-met]]
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
[[Category: bacteriochllochlorophyll]]
+
<text>to colour the structure by Evolutionary Conservation</text>
-
[[Category: bchu]]
+
</jmolCheckbox>
-
[[Category: methyltransferase]]
+
</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].
-
[[Category: s-adenosylhomocysteine]]
+
<div style="clear:both"></div>
-
[[Category: s-adenosylmethyonine]]
+
== References ==
-
[[Category: sah]]
+
<references/>
-
[[Category: sam]]
+
__TOC__
-
 
+
</StructureSection>
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:13:13 2007''
+
[[Category: Chlorobaculum tepidum TLS]]
 +
[[Category: Large Structures]]
 +
[[Category: Fukuyama K]]
 +
[[Category: Wada K]]
 +
[[Category: Yamaguchi H]]

Current revision

Crystal structure of BchU involved in bacteriochlorophyll c biosynthesis

PDB ID 1x19

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/1x19"
Personal tools