1kxz
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="1kxz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kxz, resolution 2.70Å" /> '''MT0146, the Precorri...) |
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| - | [[Image:1kxz.gif|left|200px]]<br /><applet load="1kxz" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1kxz, resolution 2.70Å" /> | ||
| - | '''MT0146, the Precorrin-6y methyltransferase (CbiT) homolog from M. Thermoautotrophicum, P1 spacegroup'''<br /> | ||
| - | == | + | ==MT0146, the Precorrin-6y methyltransferase (CbiT) homolog from M. Thermoautotrophicum, P1 spacegroup== |
| - | The CbiT and CbiE enzymes participate in the biosynthesis of vitamin B12. | + | <StructureSection load='1kxz' size='340' side='right'caption='[[1kxz]], [[Resolution|resolution]] 2.70Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1kxz]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KXZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KXZ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kxz OCA], [https://pdbe.org/1kxz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kxz RCSB], [https://www.ebi.ac.uk/pdbsum/1kxz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kxz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CBIT_METTH CBIT_METTH] Catalyzes the methylation of C-15 in cobalt-precorrin-6B followed by the decarboxylation of C-12 to form cobalt-precorrin-7 (Probable).<ref>PMID:12429089</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kx/1kxz_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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=1kxz ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The CbiT and CbiE enzymes participate in the biosynthesis of vitamin B12. They are fused together in some organisms to form a protein called CobL, which catalyzes two methylations and one decarboxylation on a precorrin intermediate. Because CbiE has sequence homology to canonical precorrin methyltransferases, CbiT was hypothesized to catalyze the decarboxylation. We herein present the crystal structure of MT0146, the CbiT homolog from Methanobacterium thermoautotrophicum. The protein shows structural similarity to Rossmann-like S-adenosyl-methionine-dependent methyltransferases, and our 1.9 A cocrystal structure shows that it binds S-adenosyl-methionine in standard geometry near a binding pocket that could accommodate a precorrin substrate. Therefore, MT0146/CbiT probably functions as a precorrin methyltransferase and represents the first enzyme identified with this activity that does not have the canonical precorrin methyltransferase fold. | ||
| - | + | The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase.,Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF Structure. 2002 Nov;10(11):1475-87. PMID:12429089<ref>PMID:12429089</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1kxz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
| - | + | [[Category: Benach J]] | |
| - | [[Category: Benach | + | [[Category: Christendat D]] |
| - | [[Category: Christendat | + | [[Category: DeTitta G]] |
| - | [[Category: DeTitta | + | [[Category: Hunt JF]] |
| - | [[Category: Hunt | + | [[Category: Keller JP]] |
| - | [[Category: Keller | + | [[Category: Smith PM]] |
| - | [[Category: Smith | + | |
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Current revision
MT0146, the Precorrin-6y methyltransferase (CbiT) homolog from M. Thermoautotrophicum, P1 spacegroup
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