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| | ==Crystal structure of C-terminal domain of precorrin-6Y C5,15-methyltransferase from Rhodobacter capsulatus== | | ==Crystal structure of C-terminal domain of precorrin-6Y C5,15-methyltransferase from Rhodobacter capsulatus== |
| - | <StructureSection load='3njr' size='340' side='right' caption='[[3njr]], [[Resolution|resolution]] 2.70Å' scene=''> | + | <StructureSection load='3njr' size='340' side='right'caption='[[3njr]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3njr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhocb Rhocb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NJR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3njr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodobacter_capsulatus_SB_1003 Rhodobacter capsulatus SB 1003]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NJR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NJR FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 2.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cobL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272942 RHOCB])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Precorrin-6B_C(5,15)-methyltransferase_(decarboxylating) Precorrin-6B C(5,15)-methyltransferase (decarboxylating)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.132 2.1.1.132] </span></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=3njr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3njr OCA], [https://pdbe.org/3njr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3njr RCSB], [https://www.ebi.ac.uk/pdbsum/3njr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3njr ProSAT]</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=3njr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3njr OCA], [http://pdbe.org/3njr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3njr RCSB], [http://www.ebi.ac.uk/pdbsum/3njr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3njr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/D5AV04_RHOCB D5AV04_RHOCB] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhocb]] | + | [[Category: Large Structures]] |
| - | [[Category: Pickersgill, R W]] | + | [[Category: Rhodobacter capsulatus SB 1003]] |
| - | [[Category: Seyedarabi, A]] | + | [[Category: Pickersgill RW]] |
| - | [[Category: Decarboxylase]] | + | [[Category: Seyedarabi A]] |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
D5AV04_RHOCB
Publication Abstract from PubMed
The biosynthesis of many vitamins and coenzymes has often proven difficult to elucidate owing to a combination of low abundance and kinetic lability of the pathway intermediates. Through a serial reconstruction of the cobalamin (vitamin B(12)) pathway in Escherichia coli and by His tagging the terminal enzyme in the reaction sequence, we have observed that many unstable intermediates can be isolated as tightly bound enzyme-product complexes. Together, these approaches have been used to extract intermediates between precorrin-4 and hydrogenobyrinic acid in their free acid form and permitted the delineation of the overall reaction catalyzed by CobL, including the formal elucidation of precorrin-7 as a metabolite. Furthermore, a substrate-carrier protein, CobE, that can also be used to stabilize some of the transient metabolic intermediates and enhance their onward transformation, has been identified. The tight association of pathway intermediates with enzymes provides evidence for a form of metabolite channeling.
An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis.,Deery E, Schroeder S, Lawrence AD, Taylor SL, Seyedarabi A, Waterman J, Wilson KS, Brown D, Geeves MA, Howard MJ, Pickersgill RW, Warren MJ Nat Chem Biol. 2012 Oct 7. doi: 10.1038/nchembio.1086. PMID:23042036[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Deery E, Schroeder S, Lawrence AD, Taylor SL, Seyedarabi A, Waterman J, Wilson KS, Brown D, Geeves MA, Howard MJ, Pickersgill RW, Warren MJ. An enzyme-trap approach allows isolation of intermediates in cobalamin biosynthesis. Nat Chem Biol. 2012 Oct 7. doi: 10.1038/nchembio.1086. PMID:23042036 doi:http://dx.doi.org/10.1038/nchembio.1086
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