1i1h
From Proteopedia
(New page: 200px<br /><applet load="1i1h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i1h, resolution 2.60Å" /> '''CRYSTAL STRUCTURE AN...) |
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| - | [[Image:1i1h.gif|left|200px]]<br /><applet load="1i1h" size=" | + | [[Image:1i1h.gif|left|200px]]<br /><applet load="1i1h" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1i1h, resolution 2.60Å" /> | caption="1i1h, resolution 2.60Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID'''<br /> | ||
==Overview== | ==Overview== | ||
| - | BACKGROUND: The crystal structure of precorrin-8x methyl mutase (CobH), an | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1I1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_denitrificans Pseudomonas denitrificans] with COJ as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1I1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_denitrificans Pseudomonas denitrificans] with <scene name='pdbligand=COJ:'>COJ</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Li, D.]] | [[Category: Li, D.]] | ||
| - | [[Category: Roessner, C | + | [[Category: Roessner, C A.]] |
| - | [[Category: Sacchettini, J | + | [[Category: Sacchettini, J C.]] |
| - | [[Category: Scott, A | + | [[Category: Scott, A I.]] |
| - | [[Category: Shipman, L | + | [[Category: Shipman, L W.]] |
[[Category: COJ]] | [[Category: COJ]] | ||
[[Category: precorrin]] | [[Category: precorrin]] | ||
[[Category: vitamin b12]] | [[Category: vitamin b12]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:04 2008'' |
Revision as of 11:07, 21 February 2008
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CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID
Overview
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.
About this Structure
1I1H is a Single protein structure of sequence from Pseudomonas denitrificans with as ligand. Active as Precorrin-8X methylmutase, with EC number 5.4.1.2 Full crystallographic information is available from OCA.
Reference
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
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