5u58: Difference between revisions

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<StructureSection load='5u58' size='340' side='right'caption='[[5u58]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
<StructureSection load='5u58' size='340' side='right'caption='[[5u58]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5u58]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19310 Atcc 19310]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U58 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5U58 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5u58]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5U58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5U58 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=TB6:[(2R)-2-HYDROXYPROPYL]PHOSPHONIC+ACID'>TB6</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]] 2.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5u57|5u57]], [[5u55|5u55]], [[5u5d|5u5d]]</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=TB6:[(2R)-2-HYDROXYPROPYL]PHOSPHONIC+ACID'>TB6</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hppE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=317 ATCC 19310])</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=5u58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u58 OCA], [https://pdbe.org/5u58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5u58 RCSB], [https://www.ebi.ac.uk/pdbsum/5u58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5u58 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/(S)-2-hydroxypropylphosphonic_acid_epoxidase (S)-2-hydroxypropylphosphonic acid epoxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.23 1.11.1.23] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5u58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5u58 OCA], [http://pdbe.org/5u58 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5u58 RCSB], [http://www.ebi.ac.uk/pdbsum/5u58 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5u58 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HPPE_PSESX HPPE_PSESX]] 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:18656958</ref> 
[https://www.uniprot.org/uniprot/HPPE_PSESX HPPE_PSESX] 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:18656958</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The broad-spectrum phosphonate antibiotic fosfomycin is currently in use for clinical treatment of infections caused by both Gram-positive and Gram-negative uropathogens. The antibiotic is biosynthesized by various streptomycetes, as well as by pseudomonads. Notably, the biosynthetic strategies used by the two genera share only two steps: the first step in which primary metabolite phosphoenolpyruvate (PEP) is converted to phosphonopyruvate (PnPy) and the terminal step in which 2-hydroxypropylphosphonate (2-HPP) is converted to fosfomycin. Otherwise, distinct enzymatic paths are employed. Here, we biochemically confirm the last two steps in the fosfomycin biosynthetic pathway of Pseudomonas syringae PB-5123, showing that Psf3 performs the reduction of 2-oxopropylphosphonate (2-OPP) to (S)-2-HPP, followed by the Psf4-catalyzed epoxidation of (S)-2-HPP to fosfomycin. Psf4 can also accept (R)-2-HPP as a substrate but instead performs an oxidation to make 2-OPP. We show that the combined activities of Psf3 and Psf4 can be used to convert racemic 2-HPP to fosfomycin in an enantioconvergent process. X-ray structures of each enzyme with bound substrates provide insights into the stereospecificity of each conversion. These studies shed light on the reaction mechanisms of the two terminal enzymes in a distinct pathway employed by pseudomonads for the production of a potent antimicrobial agent.
 
Characterization of Two Late-Stage Enzymes Involved in Fosfomycin Biosynthesis in Pseudomonads.,Olivares P, Ulrich EC, Chekan JR, van der Donk WA, Nair SK ACS Chem Biol. 2016 Dec 27. doi: 10.1021/acschembio.6b00939. PMID:27977135<ref>PMID:27977135</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5u58" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 19310]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chekan, J R]]
[[Category: Pseudomonas syringae]]
[[Category: Nair, S K]]
[[Category: Chekan JR]]
[[Category: Epoxidase]]
[[Category: Nair SK]]
[[Category: Fosfomycin]]
[[Category: Oxidase]]
[[Category: Oxidoreductase]]

Latest revision as of 17:25, 6 March 2024

Psf4 in complex with Fe2+ and (R)-2-HPPPsf4 in complex with Fe2+ and (R)-2-HPP

Structural highlights

5u58 is a 4 chain structure with sequence from Pseudomonas syringae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.7Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HPPE_PSESX 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]

See Also

References

  1. ↑ Munos JW, Moon SJ, Mansoorabadi SO, Chang W, Hong L, Yan F, Liu A, Liu HW. Purification and characterization of the epoxidase catalyzing the formation of fosfomycin from Pseudomonas syringae. Biochemistry. 2008 Aug 19;47(33):8726-35. doi: 10.1021/bi800877v. Epub 2008 Jul, 26. PMID:18656958 doi:http://dx.doi.org/10.1021/bi800877v

5u58, resolution 2.70Å

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