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| | ==GGGPS from Methanothermobacter thermautotrophicus== | | ==GGGPS from Methanothermobacter thermautotrophicus== |
| - | <StructureSection load='4mm1' size='340' side='right' caption='[[4mm1]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='4mm1' size='340' side='right'caption='[[4mm1]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4mm1]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [http://en.wikipedia.org/wiki/Metth Metth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MM1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MM1 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4mm1]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus_str._Delta_H Methanothermobacter thermautotrophicus str. Delta H]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MM1 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1GP:SN-GLYCEROL-1-PHOSPHATE'>1GP</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1GP:SN-GLYCEROL-1-PHOSPHATE'>1GP</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MTH_552 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=187420 METTH])</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=4mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mm1 OCA], [https://pdbe.org/4mm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mm1 RCSB], [https://www.ebi.ac.uk/pdbsum/4mm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mm1 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/Phosphoglycerol_geranylgeranyltransferase Phosphoglycerol geranylgeranyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.41 2.5.1.41] </span></td></tr>
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| - | <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=4mm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mm1 OCA], [http://pdbe.org/4mm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mm1 RCSB], [http://www.ebi.ac.uk/pdbsum/4mm1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mm1 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GGGPS_METTH GGGPS_METTH]] Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids (By similarity).[HAMAP-Rule:MF_00112] | + | [https://www.uniprot.org/uniprot/GGGPS_METTH GGGPS_METTH] Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids (By similarity).[HAMAP-Rule:MF_00112] |
| | <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: Escherichia coli]] | + | [[Category: Large Structures]] |
| - | [[Category: Metth]] | + | [[Category: Methanothermobacter thermautotrophicus str. Delta H]] |
| - | [[Category: Phosphoglycerol geranylgeranyltransferase]]
| + | [[Category: Babinger P]] |
| - | [[Category: Babinger, P]] | + | [[Category: Beer B]] |
| - | [[Category: Beer, B]] | + | [[Category: Guldan H]] |
| - | [[Category: Guldan, H]] | + | [[Category: Kapetaniou E]] |
| - | [[Category: Kapetaniou, E]] | + | [[Category: Kumpula EP]] |
| - | [[Category: Kumpula, E P]] | + | [[Category: Peterhoff D]] |
| - | [[Category: Peterhoff, D]] | + | [[Category: Rajendran C]] |
| - | [[Category: Rajendran, C]] | + | [[Category: Sterner R]] |
| - | [[Category: Sterner, R]] | + | [[Category: Wierenga RK]] |
| - | [[Category: Wierenga, R K]] | + | |
| - | [[Category: Gggp]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
GGGPS_METTH Prenyltransferase that catalyzes the transfer of the geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the first ether-bond-formation step in the biosynthesis of archaeal membrane lipids (By similarity).[HAMAP-Rule:MF_00112]
Publication Abstract from PubMed
Geranylgeranylglyceryl phosphate synthase (GGGPS) family enzymes catalyse the formation of an ether bond between glycerol-1-phosphate and polyprenyl diphosphates. They are essential for the biosynthesis of archaeal membrane lipids, but also occur in bacterial species, albeit with unknown physiological function. It has been known that there exist two phylogenetic groups (I and II) of GGGPS family enzymes, but a comprehensive study has been missing. We therefore visualized the variability within the family by applying a sequence similarity network, and biochemically characterized 17 representative GGGPS family enzymes regarding their catalytic activities and substrate specificities. Moreover, we present the first crystal structures of group II archaeal and bacterial enzymes. Our analysis revealed that the previously uncharacterized bacterial enzymes from group II have GGGPS activity like the archaeal enzymes and differ from the bacterial group I enzymes that are heptaprenylglyceryl phosphate synthases. The length of the isoprenoid substrate is determined in group II GGGPS enzymes by 'limiter residues' that are different from those in group I enzymes, as shown by site-directed mutagenesis. Most of the group II enzymes form hexamers. We could disrupt these hexamers to stable and catalytically active dimers by mutating a single amino acid that acts as an 'aromatic anchor'.
A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase enzyme family identifies novel members and reveals mechanisms of substrate specificity and quaternary structure organization.,Peterhoff D, Beer B, Rajendran C, Kumpula EP, Kapetaniou E, Guldan H, Wierenga RK, Sterner R, Babinger P Mol Microbiol. 2014 May;92(4):885-99. doi: 10.1111/mmi.12596. Epub 2014 Apr 16. PMID:24684232[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Peterhoff D, Beer B, Rajendran C, Kumpula EP, Kapetaniou E, Guldan H, Wierenga RK, Sterner R, Babinger P. A comprehensive analysis of the geranylgeranylglyceryl phosphate synthase enzyme family identifies novel members and reveals mechanisms of substrate specificity and quaternary structure organization. Mol Microbiol. 2014 May;92(4):885-99. doi: 10.1111/mmi.12596. Epub 2014 Apr 16. PMID:24684232 doi:http://dx.doi.org/10.1111/mmi.12596
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