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==CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID==
[[Image:1i1h.png|left|200px]]
<StructureSection load='1i1h' size='340' side='right' caption='[[1i1h]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1i1h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_denitrificans"_(christensen_1903)_bergey_et_al._1923,_nom._rejic. "pseudomonas denitrificans" (christensen 1903) bergey et al. 1923, nom. rejic.]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1I1H FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COJ:HYDROGENOBYRINIC+ACID'>COJ</scene><br>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f2v|1f2v]]</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COBH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43306 "Pseudomonas denitrificans" (Christensen 1903) Bergey et al. 1923, nom. rejic.])</td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1i1h RCSB], [http://www.ebi.ac.uk/pdbsum/1i1h PDBsum]</span></td></tr>
<table>
== 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/i1/1i1h_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


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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:11470433<ref>PMID:11470433</ref>
The line below this paragraph, containing "STRUCTURE_1i1h", creates the "Structure Box" on the page.
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===CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
 
== References ==
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The line below this paragraph, {{ABSTRACT_PUBMED_11470433}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11470433 is the PubMed ID number.
</StructureSection>
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{{ABSTRACT_PUBMED_11470433}}
 
==About this Structure==
1I1H is a 1 chain 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].
 
==Reference==
<ref group="xtra">PMID:11470433</ref><references group="xtra"/>
[[Category: Precorrin-8X methylmutase]]
[[Category: Precorrin-8X methylmutase]]
[[Category: Pseudomonas denitrificans]]
[[Category: Li, D.]]
[[Category: Li, D.]]
[[Category: Roessner, C A.]]
[[Category: Roessner, C A.]]
Line 31: Line 37:
[[Category: Scott, A I.]]
[[Category: Scott, A I.]]
[[Category: Shipman, L W.]]
[[Category: Shipman, L W.]]
[[Category: Isomerase]]
[[Category: Precorrin]]
[[Category: Precorrin]]
[[Category: Vitamin b12]]
[[Category: Vitamin b12]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:28:23 2009''

Revision as of 17:26, 28 September 2014

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"_(christensen_1903)_bergey_et_al._1923,_nom._rejic. "pseudomonas denitrificans" (christensen 1903) bergey et al. 1923, nom. rejic.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:1f2v
Gene:COBH ("Pseudomonas denitrificans" (Christensen 1903) Bergey et al. 1923, nom. rejic.)
Activity:Precorrin-8X methylmutase, with EC number 5.4.1.2
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

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

Publication Abstract from PubMed

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.

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:11470433[1]

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

References

  1. ↑ Shipman LW, Li D, Roessner CA, Scott AI, Sacchettini JC. Crystal structure of precorrin-8x methyl mutase. Structure. 2001 Jul 3;9(7):587-96. PMID:11470433

1i1h, resolution 2.60Å

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