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| | <StructureSection load='3ppf' size='340' side='right'caption='[[3ppf]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='3ppf' size='340' side='right'caption='[[3ppf]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ppf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_11006_[[candida_stellatoidea]] Atcc 11006 [[candida stellatoidea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ppf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPF FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3pph|3pph]], [[3ppc|3ppc]], [[3ppg|3ppg]]</div></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]] 2.3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CaO19.10083, CaO19.2551, MET6 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 ATCC 11006 [[Candida stellatoidea]]])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </span></td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ppf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppf OCA], [https://pdbe.org/3ppf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppf RCSB], [https://www.ebi.ac.uk/pdbsum/3ppf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppf ProSAT]</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=3ppf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppf OCA], [https://pdbe.org/3ppf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppf RCSB], [https://www.ebi.ac.uk/pdbsum/3ppf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/METE_CANAL METE_CANAL]] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.[HAMAP-Rule:MF_00172]
| + | [https://www.uniprot.org/uniprot/METE_CANAL METE_CANAL] Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.[HAMAP-Rule:MF_00172] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 3ppf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 3ppf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Methionine synthase 3D structures|Methionine synthase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]] | + | [[Category: Candida albicans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kavanagh, K]] | + | [[Category: Kavanagh K]] |
| - | [[Category: Monzingo, A F]] | + | [[Category: Monzingo AF]] |
| - | [[Category: Robertus, J D]] | + | [[Category: Robertus JD]] |
| - | [[Category: Ubhi, D]] | + | [[Category: Ubhi D]] |
| - | [[Category: Cobalamin-independent]]
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| - | [[Category: Metalloproteinase]]
| + | |
| - | [[Category: Methyltransferase]]
| + | |
| - | [[Category: Surface entropy reduction]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
METE_CANAL Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation.[HAMAP-Rule:MF_00172]
Publication Abstract from PubMed
Fungal methionine synthase, Met6p, transfers a methyl group from 5-methyl-tetrahydrofolate to homocysteine to generate methionine. The enzyme is essential to fungal growth and is a potential anti-fungal drug design target. We have characterized the enzyme from the pathogen Candida albicans but were unable to crystallize it in native form. We converted Lys103, Lys104, and Glu107 all to Tyr (Met6pY), Thr (Met6pT) and Ala (Met6pA). All variants showed wild-type kinetic activity and formed useful crystals, each with unique crystal packing. In each case the mutated residues participated in beneficial crystal contacts. We have solved the three structures at 2.0-2.8A resolution and analyzed crystal packing, active-site residues, and similarity to other known methionine synthase structures. C. albicans Met6p has a two domain structure with each of the domains having a (betaalpha)(8)-barrel fold. The barrels are arranged face-to-face and the active site is located in a cleft between the two domains. Met6p utilizes a zinc ion for catalysis that is bound in the C-terminal domain and ligated by four conserved residues: His657, Cys659, Glu679 and Cys739.
Structure of Candida albicans methionine synthase determined by employing surface residue mutagenesis.,Ubhi D, Kavanagh KL, Monzingo AF, Robertus JD Arch Biochem Biophys. 2011 Sep 1;513(1):19-26. doi:, 10.1016/j.abb.2011.06.002. Epub 2011 Jun 12. PMID:21689631[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ubhi D, Kavanagh KL, Monzingo AF, Robertus JD. Structure of Candida albicans methionine synthase determined by employing surface residue mutagenesis. Arch Biochem Biophys. 2011 Sep 1;513(1):19-26. doi:, 10.1016/j.abb.2011.06.002. Epub 2011 Jun 12. PMID:21689631 doi:10.1016/j.abb.2011.06.002
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