3ro6: Difference between revisions

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<StructureSection load='3ro6' size='340' side='right'caption='[[3ro6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3ro6' size='340' side='right'caption='[[3ro6]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ro6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Acm_1292 Acm 1292]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RO6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ro6]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus Methylococcus capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RO6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.2&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rit|3rit]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MCA1834 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=414 ACM 1292])</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=3ro6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ro6 OCA], [https://pdbe.org/3ro6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ro6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ro6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ro6 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=3ro6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ro6 OCA], [https://pdbe.org/3ro6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ro6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ro6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ro6 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/KRDE_METCA KRDE_METCA] Catalyzes the epimerization of L-Lys-L-Arg to L-Lys-D-Arg. Can also catalyze the epimerization of other cationic dipeptides, such as L-Arg-L-Arg, L-Lys-L-Lys and L-Lys-L-His, but with lower efficiency (in vitro).<ref>PMID:22392983</ref>  
The rapid advance in genome sequencing presents substantial challenges for protein functional assignment, with half or more of new protein sequences inferred from these genomes having uncertain assignments. The assignment of enzyme function in functionally diverse superfamilies represents a particular challenge, which we address through a combination of computational predictions, enzymology, and structural biology. Here we describe the results of a focused investigation of a group of enzymes in the enolase superfamily that are involved in epimerizing dipeptides. The first members of this group to be functionally characterized were Ala-Glu epimerases in Eschericiha coli and Bacillus subtilis, based on the operon context and enzymological studies; these enzymes are presumed to be involved in peptidoglycan recycling. We have subsequently studied more than 65 related enzymes by computational methods, including homology modeling and metabolite docking, which suggested that many would have divergent specificities;, i.e., they are likely to have different (unknown) biological roles. In addition to the Ala-Phe epimerase specificity reported previously, we describe the prediction and experimental verification of: (i) a new group of presumed Ala-Glu epimerases; (ii) several enzymes with specificity for hydrophobic dipeptides, including one from Cytophaga hutchinsonii that epimerizes D-Ala-D-Ala; and (iii) a small group of enzymes that epimerize cationic dipeptides. Crystal structures for certain of these enzymes further elucidate the structural basis of the specificities. The results highlight the potential of computational methods to guide experimental characterization of enzymes in an automated, large-scale fashion.
 
Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily.,Lukk T, Sakai A, Kalyanaraman C, Brown SD, Imker HJ, Song L, Fedorov AA, Fedorov EV, Toro R, Hillerich B, Seidel R, Patskovsky Y, Vetting MW, Nair SK, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP Proc Natl Acad Sci U S A. 2012 Mar 13;109(11):4122-7. Epub 2012 Mar 5. PMID:22392983<ref>PMID:22392983</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ro6" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acm 1292]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Gerlt, J A]]
[[Category: Methylococcus capsulatus]]
[[Category: Lukk, T]]
[[Category: Gerlt JA]]
[[Category: Nair, S K]]
[[Category: Lukk T]]
[[Category: Sakai, A]]
[[Category: Nair SK]]
[[Category: Song, L]]
[[Category: Sakai A]]
[[Category: Isomerase]]
[[Category: Song L]]
[[Category: Tim barrel]]

Latest revision as of 12:44, 1 March 2024

Crystal structure of Dipeptide Epimerase from Methylococcus capsulatus complexed with Mg ionCrystal structure of Dipeptide Epimerase from Methylococcus capsulatus complexed with Mg ion

Structural highlights

3ro6 is a 6 chain structure with sequence from Methylococcus capsulatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KRDE_METCA Catalyzes the epimerization of L-Lys-L-Arg to L-Lys-D-Arg. Can also catalyze the epimerization of other cationic dipeptides, such as L-Arg-L-Arg, L-Lys-L-Lys and L-Lys-L-His, but with lower efficiency (in vitro).[1]

References

  1. ↑ Lukk T, Sakai A, Kalyanaraman C, Brown SD, Imker HJ, Song L, Fedorov AA, Fedorov EV, Toro R, Hillerich B, Seidel R, Patskovsky Y, Vetting MW, Nair SK, Babbitt PC, Almo SC, Gerlt JA, Jacobson MP. Homology models guide discovery of diverse enzyme specificities among dipeptide epimerases in the enolase superfamily. Proc Natl Acad Sci U S A. 2012 Mar 13;109(11):4122-7. Epub 2012 Mar 5. PMID:22392983 doi:10.1073/pnas.1112081109

3ro6, resolution 2.20Å

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