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| | ==X-Ray Crystal Structure of 2-amino-1-hydroxyethylphosphonate-bound PhnZ== | | ==X-Ray Crystal Structure of 2-amino-1-hydroxyethylphosphonate-bound PhnZ== |
| - | <StructureSection load='4n71' size='340' side='right' caption='[[4n71]], [[Resolution|resolution]] 2.98Å' scene=''> | + | <StructureSection load='4n71' size='340' side='right'caption='[[4n71]], [[Resolution|resolution]] 2.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n71]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultured_bacterium_hf130_aepn_1 Uncultured bacterium hf130_aepn_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N71 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N71 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n71]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium_HF130_AEPn_1 Uncultured bacterium HF130_AEPn_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N71 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ODV:[(1R)-2-AMINO-1-HYDROXYETHYL]PHOSPHONIC+ACID'>ODV</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=ODV:[(1R)-2-AMINO-1-HYDROXYETHYL]PHOSPHONIC+ACID'>ODV</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n6w|4n6w]]</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=4n71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n71 OCA], [https://pdbe.org/4n71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n71 RCSB], [https://www.ebi.ac.uk/pdbsum/4n71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n71 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACU83550, ALOHA_HF130_AEPn_1_06c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=663362 uncultured bacterium HF130_AEPn_1])</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=4n71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n71 OCA], [http://pdbe.org/4n71 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n71 RCSB], [http://www.ebi.ac.uk/pdbsum/4n71 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n71 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PHNZ_UNCHF PHNZ_UNCHF] Involved in the degradation of the organophosphonate 2-aminoethylphosphonic acid (2-AEP) (Probable). Catalyzes the cleavage of the carbon-phosphorus bond of (2-amino-1-hydroxyethyl)phosphonic acid to yield glycine and phosphate through an oxidative mechanism (PubMed:22564006, PubMed:24198335, PubMed:24706911). It reacts stereospecifically with the R-enantiomer of (2-amino-1-hydroxyethyl)phosphonic acid and is also able to use (R,R)-2-amino-1-hydroxypropylphosphonate as substrate (PubMed:24706911).<ref>PMID:22564006</ref> <ref>PMID:24198335</ref> <ref>PMID:24706911</ref> <ref>PMID:19788654</ref> |
| | <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: Uncultured bacterium hf130_aepn_1]] | + | [[Category: Large Structures]] |
| - | [[Category: Boal, A K]] | + | [[Category: Uncultured bacterium HF130_AEPn_1]] |
| - | [[Category: Jr, J M.Bollinger]] | + | [[Category: Boal AK]] |
| - | [[Category: Krebs, C]] | + | [[Category: Bollinger Jr JM]] |
| - | [[Category: Lingaraju, M]] | + | [[Category: Krebs C]] |
| - | [[Category: Pandelia, M E]] | + | [[Category: Lingaraju M]] |
| - | [[Category: Woersdoerfer, B]] | + | [[Category: Pandelia M-E]] |
| - | [[Category: Yennawar, N]] | + | [[Category: Woersdoerfer B]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Yennawar N]] |
| - | [[Category: Oxygenase]]
| + | |
| Structural highlights
Function
PHNZ_UNCHF Involved in the degradation of the organophosphonate 2-aminoethylphosphonic acid (2-AEP) (Probable). Catalyzes the cleavage of the carbon-phosphorus bond of (2-amino-1-hydroxyethyl)phosphonic acid to yield glycine and phosphate through an oxidative mechanism (PubMed:22564006, PubMed:24198335, PubMed:24706911). It reacts stereospecifically with the R-enantiomer of (2-amino-1-hydroxyethyl)phosphonic acid and is also able to use (R,R)-2-amino-1-hydroxypropylphosphonate as substrate (PubMed:24706911).[1] [2] [3] [4]
Publication Abstract from PubMed
The founding members of the HD-domain protein superfamily are phosphohydrolases, and newly discovered members are generally annotated as such. However, myo-inositol oxygenase (MIOX) exemplifies a second, very different function that has evolved within the common scaffold of this superfamily. A recently discovered HD protein, PhnZ, catalyzes conversion of 2-amino-1-hydroxyethylphosphonate to glycine and phosphate, culminating a bacterial pathway for the utilization of environmentally abundant 2-aminoethylphosphonate. Using Mossbauer and EPR spectroscopies, X-ray crystallography, and activity measurements, we show here that, like MIOX, PhnZ employs a mixed-valent Fe(II)/Fe(III) cofactor for the O2-dependent oxidative cleavage of its substrate. Phylogenetic analysis suggests that many more HD proteins may catalyze yet-unknown oxygenation reactions using this hitherto exceptional Fe(II)/Fe(III) cofactor. The results demonstrate that the catalytic repertoire of the HD superfamily extends well beyond phosphohydrolysis and suggest that the mechanism used by MIOX and PhnZ may be a common strategy for oxidative C-X bond cleavage.
Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases.,Worsdorfer B, Lingaraju M, Yennawar NH, Boal AK, Krebs C, Bollinger JM Jr, Pandelia ME Proc Natl Acad Sci U S A. 2013 Nov 19;110(47):18874-9. doi:, 10.1073/pnas.1315927110. Epub 2013 Nov 6. PMID:24198335[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ McSorley FR, Wyatt PB, Martinez A, DeLong EF, Hove-Jensen B, Zechel DL. PhnY and PhnZ comprise a new oxidative pathway for enzymatic cleavage of a carbon-phosphorus bond. J Am Chem Soc. 2012 May 23;134(20):8364-7. doi: 10.1021/ja302072f. Epub 2012 May , 11. PMID:22564006 doi:http://dx.doi.org/10.1021/ja302072f
- ↑ Worsdorfer B, Lingaraju M, Yennawar NH, Boal AK, Krebs C, Bollinger JM Jr, Pandelia ME. Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases. Proc Natl Acad Sci U S A. 2013 Nov 19;110(47):18874-9. doi:, 10.1073/pnas.1315927110. Epub 2013 Nov 6. PMID:24198335 doi:http://dx.doi.org/10.1073/pnas.1315927110
- ↑ van Staalduinen LM, McSorley FR, Schiessl K, Seguin J, Wyatt PB, Hammerschmidt F, Zechel DL, Jia Z. Crystal structure of PhnZ in complex with substrate reveals a di-iron oxygenase mechanism for catabolism of organophosphonates. Proc Natl Acad Sci U S A. 2014 Apr 8;111(14):5171-6. doi:, 10.1073/pnas.1320039111. Epub 2014 Mar 21. PMID:24706911 doi:http://dx.doi.org/10.1073/pnas.1320039111
- ↑ Martinez A, Tyson GW, Delong EF. Widespread known and novel phosphonate utilization pathways in marine bacteria revealed by functional screening and metagenomic analyses. Environ Microbiol. 2010 Jan;12(1):222-38. doi: 10.1111/j.1462-2920.2009.02062.x. , Epub 2009 Sep 29. PMID:19788654 doi:http://dx.doi.org/10.1111/j.1462-2920.2009.02062.x
- ↑ Worsdorfer B, Lingaraju M, Yennawar NH, Boal AK, Krebs C, Bollinger JM Jr, Pandelia ME. Organophosphonate-degrading PhnZ reveals an emerging family of HD domain mixed-valent diiron oxygenases. Proc Natl Acad Sci U S A. 2013 Nov 19;110(47):18874-9. doi:, 10.1073/pnas.1315927110. Epub 2013 Nov 6. PMID:24198335 doi:http://dx.doi.org/10.1073/pnas.1315927110
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