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[[Image:1i1h.gif|left|200px]]


{{Structure
==CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID==
|PDB= 1i1h |SIZE=350|CAPTION= <scene name='initialview01'>1i1h</scene>, resolution 2.60&Aring;
<StructureSection load='1i1h' size='340' side='right'caption='[[1i1h]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=COJ:HYDROGENOBYRINIC ACID'>COJ</scene>
<table><tr><td colspan='2'>[[1i1h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_denitrificans_(nom._rej.) Pseudomonas denitrificans (nom. rej.)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I1H FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Precorrin-8X_methylmutase Precorrin-8X methylmutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.1.2 5.4.1.2]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
|GENE= COBH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43306 Pseudomonas denitrificans])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COJ:HYDROGENOBYRINIC+ACID'>COJ</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=1i1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1h OCA], [https://pdbe.org/1i1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i1h RCSB], [https://www.ebi.ac.uk/pdbsum/1i1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1h ProSAT]</span></td></tr>
 
</table>
'''CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID'''
== Function ==
 
[https://www.uniprot.org/uniprot/COBH_SINSX COBH_SINSX] Catalyzes the conversion of precorrin-8X to hydrogenobyrinate.<ref>PMID:1732194</ref>
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
BACKGROUND: The crystal structure of precorrin-8x methyl mutase (CobH), an enzyme of the aerobic pathway to vitamin B12, provides evidence that the mechanism for methyl migration can plausibly be regarded as an allowed [1,5]-sigmatropic shift of a methyl group from C-11 to C-12 at the C ring of precorrin-8x to afford hydrogenobyrinic acid. RESULTS: The dimeric structure of CobH creates a set of shared active sites that readily discriminate between different tautomers of precorrin-8x and select a discrete tautomer for sigmatropic rearrangement. The active site contains a strictly conserved histidine residue close to the site of methyl migration in ring C of the substrate. CONCLUSION: Analysis of the structure with bound product suggests that the [1,5]-sigmatropic shift proceeds by protonation of the ring C nitrogen, leading to subsequent methyl migration.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/1i1h_consurf.spt"</scriptWhenChecked>
1I1H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_denitrificans Pseudomonas denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1H OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
Crystal structure of precorrin-8x methyl mutase., Shipman LW, Li D, Roessner CA, Scott AI, Sacchettini JC, Structure. 2001 Jul 3;9(7):587-96. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11470433 11470433]
</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=1i1h ConSurf].
[[Category: Precorrin-8X methylmutase]]
<div style="clear:both"></div>
[[Category: Pseudomonas denitrificans]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Li, D.]]
__TOC__
[[Category: Roessner, C A.]]
</StructureSection>
[[Category: Sacchettini, J C.]]
[[Category: Large Structures]]
[[Category: Scott, A I.]]
[[Category: Li D]]
[[Category: Shipman, L W.]]
[[Category: Roessner CA]]
[[Category: COJ]]
[[Category: Sacchettini JC]]
[[Category: precorrin]]
[[Category: Scott AI]]
[[Category: vitamin b12]]
[[Category: Shipman LW]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:44:18 2008''

Latest revision as of 10:31, 7 February 2024

CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACIDCRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID

Structural highlights

1i1h is a 1 chain structure with sequence from Pseudomonas denitrificans (nom. rej.). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COBH_SINSX Catalyzes the conversion of precorrin-8X to hydrogenobyrinate.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Thibaut D, Couder M, Famechon A, Debussche L, Cameron B, Crouzet J, Blanche F. The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed by the cobH gene product with precorrin-8x as the substrate. J Bacteriol. 1992 Feb;174(3):1043-9. PMID:1732194 doi:10.1128/jb.174.3.1043-1049.1992

1i1h, resolution 2.60Å

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