View source for 2yg3


==Structure-based redesign of cofactor binding in Putrescine Oxidase: wild type enzyme==
<StructureSection load='2yg3' size='340' side='right'caption='[[2yg3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2yg3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YG3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YG3 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2yg3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yg3 OCA], [https://pdbe.org/2yg3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yg3 RCSB], [https://www.ebi.ac.uk/pdbsum/2yg3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yg3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B0F9F6_RHOER B0F9F6_RHOER] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Putrescine oxidase (PuO) from Rhodococcus erythropolis is a soluble homodimeric flavoprotein, which oxidizes small aliphatic diamines. In this study, we report the crystal structures and cofactor binding properties of wild-type and mutant enzymes. From a structural viewpoint, PuO closely resembles the sequence-related human monoamine oxidases A and B. This similarity is striking in the flavin-binding site even if PuO does not covalently bind the cofactor as do the monoamine oxidases. A remarkable conserved feature is the cis peptide conformation of the Tyr residue whose conformation is important for substrate recognition in the active site cavity. The structure of PuO in complex with the reaction product reveals that Glu324 is crucial in recognizing the terminal amino group of the diamine substrate and explains the narrow substrate specificity of the enzyme. The structural analysis also provides clues for identification of residues that are responsible for the competitive binding of ADP versus FAD ( approximately 50% of wild-type PuO monomers isolated are occupied by ADP instead of FAD). By replacing Pro15, which is part of the dinucleotide-binding domain, enzyme preparations were obtained that are almost 100% in the FAD-bound form. Furthermore, mutants have been designed and prepared that form a covalent 8alpha-S-cysteinyl-FAD linkage. These data provide new insights into the molecular basis for substrate recognition in amine oxidases and demonstrate that engineering of flavoenzymes to introduce covalent linkage with the cofactor is a possible route to develop more stable protein molecules, better suited for biocatalytic purposes.

Structure-based redesign of cofactor binding in putrescine oxidase.,Kopacz MM, Rovida S, van Duijn E, Fraaije MW, Mattevi A Biochemistry. 2011 May 17;50(19):4209-17. Epub 2011 Apr 21. PMID:21486042<ref>PMID:21486042</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2yg3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodococcus erythropolis]]
[[Category: Fraaije MW]]
[[Category: Kopacz MM]]
[[Category: Mattevi A]]
[[Category: Rovida S]]
[[Category: Van Duijn E]]