5ll2: Difference between revisions
New page: '''Unreleased structure''' The entry 5ll2 is ON HOLD Authors: Reiser, J.-B., Awad, R., Gans, P. Description: Structure of Isoleucine 2-epimerase from Lactobacillus buchneri (apo form) ... |
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The | ==Structure of Isoleucine 2-epimerase from Lactobacillus buchneri (apo form)== | ||
<StructureSection load='5ll2' size='340' side='right'caption='[[5ll2]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ll2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lentilactobacillus_buchneri Lentilactobacillus buchneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LL2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LL2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</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=5ll2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ll2 OCA], [https://pdbe.org/5ll2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ll2 RCSB], [https://www.ebi.ac.uk/pdbsum/5ll2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ll2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ILE2E_LENBU ILE2E_LENBU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The isoleucine 2-epimerase from Lactobacillus buchneri has been previously identified and characterized to catalyze the pyridoxal 5'-phosphate (PLP)-dependent racemization and epimerization of a broad spectrum of nonpolar amino acids from L- to D-form and vice versa, in particular isoleucine. In this study, crystal structures of both native and PLP-complex forms of this racemase are presented at 2.6 and 2.15 A resolution, respectively. Both structures show that the protein belongs to the fold-type I subgroup of PLP-dependent enzymes and is very close to aminobutyrate aminotransferases family, as it has been suspected because of their sequence homology. The extensive structural comparison with fold-type I enzymes with known amino acid racemization activities, including the alpha-amino-epsilon-caprolactam racemase from Achromobacter obae and the cystathionine beta-lyase from Escherichia coli, allows us to identify the active site residues responsible for its nonpolar amino acid recognition and reactivity specificity. Our observations also suggest that the racemization reaction by the fold-type I racemases may generally occur thanks to a revised two-base mechanism. Lastly, both structures reveal details on the conformational changes provoked by PLP binding that suggest an induced fit of the active site "entrance door", necessary to accommodate PLP and substrate molecules. | |||
Structural insights into the substrate recognition and reaction specificity of the PLP-dependent fold-type I isoleucine 2-epimerase from Lactobacillus buchneri.,Awad R, Gans P, Reiser JB Biochimie. 2017 Mar 23. pii: S0300-9084(16)30277-2. doi:, 10.1016/j.biochi.2017.03.015. PMID:28344038<ref>PMID:28344038</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5ll2" style="background-color:#fffaf0;"></div> | ||
[[Category: Gans | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Lentilactobacillus buchneri]] | |||
[[Category: Awad R]] | |||
[[Category: Gans P]] | |||
[[Category: Reiser J-B]] | |||
Latest revision as of 21:32, 18 October 2023
Structure of Isoleucine 2-epimerase from Lactobacillus buchneri (apo form)Structure of Isoleucine 2-epimerase from Lactobacillus buchneri (apo form)
Structural highlights
FunctionPublication Abstract from PubMedThe isoleucine 2-epimerase from Lactobacillus buchneri has been previously identified and characterized to catalyze the pyridoxal 5'-phosphate (PLP)-dependent racemization and epimerization of a broad spectrum of nonpolar amino acids from L- to D-form and vice versa, in particular isoleucine. In this study, crystal structures of both native and PLP-complex forms of this racemase are presented at 2.6 and 2.15 A resolution, respectively. Both structures show that the protein belongs to the fold-type I subgroup of PLP-dependent enzymes and is very close to aminobutyrate aminotransferases family, as it has been suspected because of their sequence homology. The extensive structural comparison with fold-type I enzymes with known amino acid racemization activities, including the alpha-amino-epsilon-caprolactam racemase from Achromobacter obae and the cystathionine beta-lyase from Escherichia coli, allows us to identify the active site residues responsible for its nonpolar amino acid recognition and reactivity specificity. Our observations also suggest that the racemization reaction by the fold-type I racemases may generally occur thanks to a revised two-base mechanism. Lastly, both structures reveal details on the conformational changes provoked by PLP binding that suggest an induced fit of the active site "entrance door", necessary to accommodate PLP and substrate molecules. Structural insights into the substrate recognition and reaction specificity of the PLP-dependent fold-type I isoleucine 2-epimerase from Lactobacillus buchneri.,Awad R, Gans P, Reiser JB Biochimie. 2017 Mar 23. pii: S0300-9084(16)30277-2. doi:, 10.1016/j.biochi.2017.03.015. PMID:28344038[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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