3pot: Difference between revisions

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[[Image:3pot.jpg|left|200px]]


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==Structural analysis of a Ni(III)-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis==
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<StructureSection load='3pot' size='340' side='right'caption='[[3pot]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3pot]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_marburgensis Methanothermobacter marburgensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3POT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3POT FirstGlance]. <br>
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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]] 1.2&#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=06C:IODOMETHANE'>06C</scene>, <scene name='pdbligand=AGM:5-METHYL-ARGININE'>AGM</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=GL3:THIOGLYCIN'>GL3</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGN:2-METHYL-GLUTAMINE'>MGN</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</scene>, <scene name='pdbligand=TXZ:O-PHOSPHONO-N-(6-SULFANYLHEXANOYL)-L-THREONINE'>TXZ</scene></td></tr>
{{STRUCTURE_3pot|  PDB=3pot  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pot OCA], [https://pdbe.org/3pot PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pot RCSB], [https://www.ebi.ac.uk/pdbsum/3pot PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pot ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MCRA_METTM MCRA_METTM] Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We present the 1.2 A resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 A proximal of the Ni atom of the MCR coenzyme F(430). A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel.


===Structural analysis of a Ni(III)-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis===
Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis.,Cedervall PE, Dey M, Li X, Sarangi R, Hedman B, Ragsdale SW, Wilmot CM J Am Chem Soc. 2011 Mar 25. PMID:21438550<ref>PMID:21438550</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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{{ABSTRACT_PUBMED_21438550}}
 
==About this Structure==
[[3pot]] is a 6 chain structure of [[Cytochrome P450]] with sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_marburgensis Methanothermobacter marburgensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3POT OCA].


==See Also==
==See Also==
*[[Cytochrome P450]]
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:21438550</ref><references group="xtra"/>
__TOC__
[[Category: Coenzyme-B sulfoethylthiotransferase]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Methanothermobacter marburgensis]]
[[Category: Methanothermobacter marburgensis]]
[[Category: Cedervall, P E.]]
[[Category: Cedervall PE]]
[[Category: Wilmot, C M.]]
[[Category: Wilmot CM]]

Latest revision as of 12:58, 6 September 2023

Structural analysis of a Ni(III)-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensisStructural analysis of a Ni(III)-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis

Structural highlights

3pot is a 6 chain structure with sequence from Methanothermobacter marburgensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.2Å
Ligands:, , , , , , , , , , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MCRA_METTM Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide.

Publication Abstract from PubMed

We present the 1.2 A resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 A proximal of the Ni atom of the MCR coenzyme F(430). A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel.

Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis.,Cedervall PE, Dey M, Li X, Sarangi R, Hedman B, Ragsdale SW, Wilmot CM J Am Chem Soc. 2011 Mar 25. PMID:21438550[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Cedervall PE, Dey M, Li X, Sarangi R, Hedman B, Ragsdale SW, Wilmot CM. Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis. J Am Chem Soc. 2011 Mar 25. PMID:21438550 doi:10.1021/ja110492p

3pot, resolution 1.20Å

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