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| | <StructureSection load='6mde' size='340' side='right'caption='[[6mde]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='6mde' size='340' side='right'caption='[[6mde]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mde]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43340_[[methanococcus_frisius_blotevogel_et_al._1986]] Atcc 43340 [[methanococcus frisius blotevogel et al. 1986]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MDE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mde]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanosarcina_mazei Methanosarcina mazei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MDE 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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MEV:(R)-MEVALONATE'>MEV</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]] 2.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mvk, MM_1762 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2209 ATCC 43340 [[Methanococcus frisius Blotevogel et al. 1986]]])</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=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MEV:(R)-MEVALONATE'>MEV</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Mevalonate_kinase Mevalonate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.36 2.7.1.36] </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=6mde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mde OCA], [https://pdbe.org/6mde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mde RCSB], [https://www.ebi.ac.uk/pdbsum/6mde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mde 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=6mde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mde OCA], [http://pdbe.org/6mde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mde RCSB], [http://www.ebi.ac.uk/pdbsum/6mde PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mde ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q8PW39_METMA Q8PW39_METMA]] Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.[HAMAP-Rule:MF_00217] | + | [https://www.uniprot.org/uniprot/Q8PW39_METMA Q8PW39_METMA] Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.[HAMAP-Rule:MF_00217] |
| | <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 6mde" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6mde" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Mevalonate kinase|Mevalonate kinase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Mevalonate kinase]] | + | [[Category: Methanosarcina mazei]] |
| - | [[Category: Kung, Y]] | + | [[Category: Kung Y]] |
| - | [[Category: Miller, B R]] | + | [[Category: Miller BR]] |
| - | [[Category: Kinase]]
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| - | [[Category: Transferase]]
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| Structural highlights
Function
Q8PW39_METMA Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.[HAMAP-Rule:MF_00217]
Publication Abstract from PubMed
Mevalonate kinase (MK) is a key enzyme of the mevalonate pathway, which produces the biosynthetic precursors for steroids, including cholesterol, and isoprenoids, the largest class of natural products. Currently available crystal structures of MK from different organisms depict the enzyme in its unbound, substrate-bound, and inhibitor-bound forms; however, until now no structure has yet been determined of MK bound to its product, 5-phosphomevalonate. Here, we present crystal structures of mevalonate-bound and 5-phosphomevalonate-bound MK from Methanosarcina mazei (MmMK), a methanogenic archaeon. In contrast to the prior structure of a eukaryotic MK bound with mevalonate, we find a striking lack of direct interactions between this archaeal MK and its substrate. Further, these two MmMK structures join the prior structure of the apoenzyme to complete the first suite of structural snapshots that depict unbound, substrate-bound, and product-bound forms of the same MK. With this collection of structures, we now provide additional insight into the catalytic mechanism of this biologically essential enzyme.
Structural insight into substrate and product binding in an archaeal mevalonate kinase.,Miller BR, Kung Y PLoS One. 2018 Dec 6;13(12):e0208419. doi: 10.1371/journal.pone.0208419., eCollection 2018. PMID:30521590[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Miller BR, Kung Y. Structural insight into substrate and product binding in an archaeal mevalonate kinase. PLoS One. 2018 Dec 6;13(12):e0208419. doi: 10.1371/journal.pone.0208419., eCollection 2018. PMID:30521590 doi:http://dx.doi.org/10.1371/journal.pone.0208419
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