1i1h: Difference between revisions
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== Structural highlights == | == 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> | <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>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COJ:HYDROGENOBYRINIC+ACID'>COJ</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f2v|1f2v]]</td></tr> | <tr id='related'><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 id='gene'><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 id='activity'><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> | <tr id='resources'><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> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/COBH_PSEDE COBH_PSEDE]] Catalyzes the conversion of precorrin-8X to hydrogenobyrinic acid; a methyl migration reaction during the transformation of precorrin-3 to form cobyrinic acid. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Precorrin-8X methylmutase]] | [[Category: Precorrin-8X methylmutase]] | ||
[[Category: Li, D | [[Category: Li, D]] | ||
[[Category: Roessner, C A | [[Category: Roessner, C A]] | ||
[[Category: Sacchettini, J C | [[Category: Sacchettini, J C]] | ||
[[Category: Scott, A I | [[Category: Scott, A I]] | ||
[[Category: Shipman, L W | [[Category: Shipman, L W]] | ||
[[Category: Isomerase]] | [[Category: Isomerase]] | ||
[[Category: Precorrin]] | [[Category: Precorrin]] | ||
[[Category: Vitamin b12]] | [[Category: Vitamin b12]] | ||
Revision as of 13:59, 25 December 2014
CRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACIDCRYSTAL STRUCTURE ANALYSIS OF PRECORRIN-8X METHYLMUTASE COMPLEX WITH HYDROGENOBYRINIC ACID
Structural highlights
Function[COBH_PSEDE] Catalyzes the conversion of precorrin-8X to hydrogenobyrinic acid; a methyl migration reaction during the transformation of precorrin-3 to form cobyrinic acid. 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 PubMedBACKGROUND: 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 |
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