1i1h: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1i1h' size='340' side='right'caption='[[1i1h]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='1i1h' size='340' side='right'caption='[[1i1h]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== 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://proteopedia.org/fgij/fg.htm?mol=1I1H FirstGlance]. <br>
<table><tr><td colspan='2'>[[1i1h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_denitrificans_(nom._rej.) Pseudomonas denitrificans (nom. rej.)]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1I1H FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COJ:HYDROGENOBYRINIC+ACID'>COJ</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f2v|1f2v]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COJ:HYDROGENOBYRINIC+ACID'>COJ</scene></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 id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1h OCA], [https://pdbe.org/1i1h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i1h RCSB], [https://www.ebi.ac.uk/pdbsum/1i1h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1h ProSAT]</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=5.4.99.61 5.4.99.61] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1i1h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i1h OCA], [http://pdbe.org/1i1h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1i1h RCSB], [http://www.ebi.ac.uk/pdbsum/1i1h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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.  
[https://www.uniprot.org/uniprot/COBH_SINSX COBH_SINSX] Catalyzes the conversion of precorrin-8X to hydrogenobyrinate.<ref>PMID:1732194</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 22: Line 20:
</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/main_output.php?pdb_ID=1i1h ConSurf].
</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/main_output.php?pdb_ID=1i1h ConSurf].
<div style="clear:both"></div>
<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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1i1h" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
Line 36: Line 25:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Precorrin-8X methylmutase]]
[[Category: Li D]]
[[Category: Li, D]]
[[Category: Roessner CA]]
[[Category: Roessner, C A]]
[[Category: Sacchettini JC]]
[[Category: Sacchettini, J C]]
[[Category: Scott AI]]
[[Category: Scott, A I]]
[[Category: Shipman LW]]
[[Category: Shipman, L W]]
[[Category: Isomerase]]
[[Category: Precorrin]]
[[Category: Vitamin b12]]

Latest revision as of 10:31, 7 February 2024

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 (nom. rej.). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

COBH_SINSX Catalyzes the conversion of precorrin-8X to hydrogenobyrinate.[1]

Evolutionary Conservation

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

References

  1. ↑ Thibaut D, Couder M, Famechon A, Debussche L, Cameron B, Crouzet J, Blanche F. The final step in the biosynthesis of hydrogenobyrinic acid is catalyzed by the cobH gene product with precorrin-8x as the substrate. J Bacteriol. 1992 Feb;174(3):1043-9. PMID:1732194 doi:10.1128/jb.174.3.1043-1049.1992

1i1h, resolution 2.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1i1h&oldid=4044739"