1i1h: Difference between revisions
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|PDB= 1i1h |SIZE=350|CAPTION= <scene name='initialview01'>1i1h</scene>, resolution 2.60Å | |PDB= 1i1h |SIZE=350|CAPTION= <scene name='initialview01'>1i1h</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=COJ:HYDROGENOBYRINIC ACID'>COJ</scene> | |LIGAND= <scene name='pdbligand=COJ:HYDROGENOBYRINIC+ACID'>COJ</scene> | ||
|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] | |ACTIVITY= <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> | ||
|GENE= COBH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43306 Pseudomonas denitrificans]) | |GENE= COBH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43306 Pseudomonas denitrificans]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1f2v|1F2V]] | |||
|RESOURCES=<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.ebi.ac.uk/pdbsum/1i1h PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i1h RCSB]</span> | |||
}} | }} | ||
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[[Category: Scott, A I.]] | [[Category: Scott, A I.]] | ||
[[Category: Shipman, L W.]] | [[Category: Shipman, L W.]] | ||
[[Category: precorrin]] | [[Category: precorrin]] | ||
[[Category: vitamin b12]] | [[Category: vitamin b12]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:13:23 2008'' | ||
Revision as of 21:13, 30 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | COBH (Pseudomonas denitrificans) | ||||||
| Activity: | Precorrin-8X methylmutase, with EC number 5.4.1.2 | ||||||
| Related: | 1F2V
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID
OverviewOverview
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 StructureAbout this Structure
1I1H is a Single protein structure of sequence from Pseudomonas denitrificans. Full crystallographic information is available from OCA.
ReferenceReference
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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