1f2v: Difference between revisions
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'''CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE OF AEROBIC VITAMIN B12 SYNTHESIS''' | {{Structure | ||
|PDB= 1f2v |SIZE=350|CAPTION= <scene name='initialview01'>1f2v</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= | |||
|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] | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE OF AEROBIC VITAMIN B12 SYNTHESIS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1F2V is a [ | 1F2V 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=1F2V OCA]. | ||
==Reference== | ==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:[http:// | 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] | ||
[[Category: Precorrin-8X methylmutase]] | [[Category: Precorrin-8X methylmutase]] | ||
[[Category: Pseudomonas denitrificans]] | [[Category: Pseudomonas denitrificans]] | ||
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[[Category: doubly wound sheet]] | [[Category: doubly wound sheet]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:36 2008'' | ||
Revision as of 09:03, 20 March 2008
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| 1f2v, resolution 2.1Å | |||||||||||||
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| Activity: | Precorrin-8X methylmutase, with EC number 5.4.1.2 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE OF AEROBIC VITAMIN B12 SYNTHESIS
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
1F2V is a Single protein structure of sequence from Pseudomonas denitrificans. 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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