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| | ==Crystal Structure of FeII HppE in Complex with Substrate form 1== | | ==Crystal Structure of FeII HppE in Complex with Substrate form 1== |
| - | <StructureSection load='1zz7' size='340' side='right' caption='[[1zz7]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='1zz7' size='340' side='right'caption='[[1zz7]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zz7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_wedmorensis"_milard_and_burr_1926 "actinomyces wedmorensis" milard and burr 1926]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZZ7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZZ7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zz7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_wedmorensis Streptomyces wedmorensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZZ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZZ7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=S0H:(S)-2-HYDROXYPROPYLPHOSPHONIC+ACID'>S0H</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zz6|1zz6]], [[1zz8|1zz8]], [[1zz9|1zz9]], [[1zzb|1zzb]], [[1zzc|1zzc]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=S0H:(S)-2-HYDROXYPROPYLPHOSPHONIC+ACID'>S0H</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fom4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=43759 "Actinomyces wedmorensis" Milard and Burr 1926])</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=1zz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zz7 OCA], [https://pdbe.org/1zz7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zz7 RCSB], [https://www.ebi.ac.uk/pdbsum/1zz7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zz7 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=1zz7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zz7 OCA], [http://pdbe.org/1zz7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zz7 RCSB], [http://www.ebi.ac.uk/pdbsum/1zz7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zz7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HPPE_STRWE HPPE_STRWE] Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic.<ref>PMID:16015285</ref> <ref>PMID:16186494</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1zz7" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1zz7" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Epoxidase 3D structures|Epoxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Actinomyces wedmorensis milard and burr 1926]] | + | [[Category: Large Structures]] |
| - | [[Category: Drennan, C L]] | + | [[Category: Streptomyces wedmorensis]] |
| - | [[Category: Higgins, L J]] | + | [[Category: Drennan CL]] |
| - | [[Category: Liu, H W]] | + | [[Category: Higgins LJ]] |
| - | [[Category: Liu, P]] | + | [[Category: Liu HW]] |
| - | [[Category: Yan, F]] | + | [[Category: Liu P]] |
| - | [[Category: Cupin]]
| + | [[Category: Yan F]] |
| - | [[Category: Mononuclear iron enzyme]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Substrate-enzyme complex]]
| + | |
| Structural highlights
Function
HPPE_STRWE Non-heme-dependent dioxygenase that catalyzes the oxidative epoxidation of (S)-2-hydroxypropylphosphonate into (1R,2S)-epoxypropylphosphonate, the final step in the biosynthesis of fosfomycin antibiotic.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The biosynthetic pathway of the clinically important antibiotic fosfomycin uses enzymes that catalyse reactions without precedent in biology. Among these is hydroxypropylphosphonic acid epoxidase, which represents a new subfamily of non-haem mononuclear iron enzymes. Here we present six X-ray structures of this enzyme: the apoenzyme at 2.0 A resolution; a native Fe(II)-bound form at 2.4 A resolution; a tris(hydroxymethyl)aminomethane-Co(II)-enzyme complex structure at 1.8 A resolution; a substrate-Co(II)-enzyme complex structure at 2.5 A resolution; and two substrate-Fe(II)-enzyme complexes at 2.1 and 2.3 A resolution. These structural data lead us to suggest how this enzyme is able to recognize and respond to its substrate with a conformational change that protects the radical-based intermediates formed during catalysis. Comparisons with other family members suggest why substrate binding is able to prime iron for dioxygen binding in the absence of alpha-ketoglutarate (a co-substrate required by many mononuclear iron enzymes), and how the unique epoxidation reaction of hydroxypropylphosphonic acid epoxidase may occur.
Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme.,Higgins LJ, Yan F, Liu P, Liu HW, Drennan CL Nature. 2005 Oct 6;437(7060):838-44. Epub 2005 Jul 13. PMID:16015285[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Higgins LJ, Yan F, Liu P, Liu HW, Drennan CL. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature. 2005 Oct 6;437(7060):838-44. Epub 2005 Jul 13. PMID:16015285 doi:http://dx.doi.org/10.1038/nature03924
- ↑ McLuskey K, Cameron S, Hammerschmidt F, Hunter WN. Structure and reactivity of hydroxypropylphosphonic acid epoxidase in fosfomycin biosynthesis by a cation- and flavin-dependent mechanism. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14221-6. Epub 2005 Sep 26. PMID:16186494
- ↑ Higgins LJ, Yan F, Liu P, Liu HW, Drennan CL. Structural insight into antibiotic fosfomycin biosynthesis by a mononuclear iron enzyme. Nature. 2005 Oct 6;437(7060):838-44. Epub 2005 Jul 13. PMID:16015285 doi:http://dx.doi.org/10.1038/nature03924
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