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4n71
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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" 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.984Å</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='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='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> | ||
</table> | </table> | ||
== Function == | == 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> | [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;"> | ||
| - | == 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. | ||
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| - | 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<ref>PMID:24198335</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4n71" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
X-Ray Crystal Structure of 2-amino-1-hydroxyethylphosphonate-bound PhnZ
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