5lfd: Difference between revisions
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<StructureSection load='5lfd' size='340' side='right'caption='[[5lfd]], [[Resolution|resolution]] 2.15Å' scene=''> | <StructureSection load='5lfd' size='340' side='right'caption='[[5lfd]], [[Resolution|resolution]] 2.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lfd]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5lfd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_fluorescens Pseudomonas fluorescens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LFD FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lfd OCA], [https://pdbe.org/5lfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lfd RCSB], [https://www.ebi.ac.uk/pdbsum/5lfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lfd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/E3SAZ9_PSEFL E3SAZ9_PSEFL] | |||
<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: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Cendron | [[Category: Pseudomonas fluorescens]] | ||
[[Category: Liuzzi | [[Category: Cendron l]] | ||
[[Category: Maccacaro | [[Category: Liuzzi A]] | ||
[[Category: Percudani | [[Category: Maccacaro E]] | ||
[[Category: Puggioni | [[Category: Percudani R]] | ||
[[Category: Ramazzina | [[Category: Puggioni V]] | ||
[[Category: Secchi | [[Category: Ramazzina I]] | ||
[[Category: Zanotti | [[Category: Secchi A]] | ||
[[Category: Zanotti G]] | |||
Latest revision as of 11:58, 11 October 2023
Crystal structure of allantoin racemase from Pseudomonas fluorescens AllRCrystal structure of allantoin racemase from Pseudomonas fluorescens AllR
Structural highlights
FunctionPublication Abstract from PubMedThe S enantiomer of allantoin is an intermediate of purine degradation in several organisms and the final product of uricolysis in nonhominoid mammals. Bioinformatics indicated that proteins of the Asp/Glu racemase superfamily could be responsible for the allantoin racemase (AllR) activity originally described in Pseudomonas species. In these proteins, a cysteine of the catalytic dyad is substituted with glycine, yet the recombinant enzyme displayed racemization activity with a similar efficiency (kcat/KM approximately 5 x 104 M-1 s-1) for the R and S enantiomers of allantoin. The protein crystal structure identified a glutamate residue located three residues downstream (E78) that can functionally replace the missing cysteine; the catalytic role of E78 was confirmed by site-directed mutagenesis. Allantoin can undergo racemization through formation of a bicyclic intermediate (faster) or proton exchange at the chiral center (slower). By monitoring the two alternative mechanisms by 13C and 1H nuclear magnetic resonance, we found that the velocity of the faster reaction is unaffected by the enzyme, whereas the velocity of the slower reaction is increased by 7 orders of magnitude. Protein phylogenies trace the origin of the racemization mechanism in enzymes acting on glutamate, a substrate for which proton exchange is the only viable reaction mechanism. This mechanism was inherited by allantoin racemase through divergent evolution and conserved in spite of the substitution of catalytic residues. The Structure and Function of a Microbial Allantoin Racemase Reveal the Origin and Conservation of a Catalytic Mechanism.,Cendron L, Ramazzina I, Puggioni V, Maccacaro E, Liuzzi A, Secchi A, Zanotti G, Percudani R Biochemistry. 2016 Nov 22;55(46):6421-6432. Epub 2016 Nov 7. PMID:27797489[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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