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==Crystal structure of the Candida albicans methionine synthase by surface entropy reduction, alanine variant with zinc==
==Crystal structure of the Candida albicans methionine synthase by surface entropy reduction, alanine variant with zinc==
<StructureSection load='3ppg' size='340' side='right' caption='[[3ppg]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
<StructureSection load='3ppg' size='340' side='right'caption='[[3ppg]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ppg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PPG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PPG FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ppg]] 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=3PPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PPG FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ppc|3ppc]], [[3ppf|3ppf]], [[3pph|3pph]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CaO19.10083, CaO19.2551, MET6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 Candida albicans])</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=3ppg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppg OCA], [https://pdbe.org/3ppg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ppg RCSB], [https://www.ebi.ac.uk/pdbsum/3ppg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ppg ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </span></td></tr>
</table>
<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=3ppg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ppg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ppg RCSB], [http://www.ebi.ac.uk/pdbsum/3ppg PDBsum]</span></td></tr>
== Function ==
<table>
[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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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<ref>PMID:21689631</ref>
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<ref>PMID:21689631</ref>


From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 3ppg" 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: Candida albicans]]
[[Category: Kavanagh, K.]]
[[Category: Large Structures]]
[[Category: Monzingo, A F.]]
[[Category: Kavanagh K]]
[[Category: Robertus, J D.]]
[[Category: Monzingo AF]]
[[Category: Ubhi, D.]]
[[Category: Robertus JD]]
[[Category: Cobalamin-independent]]
[[Category: Ubhi D]]
[[Category: Metalloproteinase]]
[[Category: Methyltransferase]]
[[Category: Surface entropy reduction]]
[[Category: Transferase]]

Latest revision as of 12:58, 6 September 2023

Crystal structure of the Candida albicans methionine synthase by surface entropy reduction, alanine variant with zincCrystal structure of the Candida albicans methionine synthase by surface entropy reduction, alanine variant with zinc

Structural highlights

3ppg is a 1 chain structure with sequence from Candida albicans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.98Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

  1. 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

3ppg, resolution 1.98Å

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