3we0: Difference between revisions

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<StructureSection load='3we0' size='340' side='right'caption='[[3we0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3we0' size='340' side='right'caption='[[3we0]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3we0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Achromobacter_georgiopolitanum Achromobacter georgiopolitanum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WE0 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3we0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WE0 FirstGlance]. <br>
</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></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]] 1.9&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">laao ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Achromobacter georgiopolitanum])</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></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] </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=3we0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3we0 OCA], [https://pdbe.org/3we0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3we0 RCSB], [https://www.ebi.ac.uk/pdbsum/3we0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3we0 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=3we0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3we0 OCA], [https://pdbe.org/3we0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3we0 RCSB], [https://www.ebi.ac.uk/pdbsum/3we0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3we0 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/B3IVI6_PSEPU B3IVI6_PSEPU]
In this study, it was shown for the first time that l-amino acid oxidase of Pseudomonas sp. AIU813, renamed as l-amino acid oxidase/monooxygenase (l-AAO/MOG), exhibits l-lysine 2-monooxygenase as well as oxidase activity. l-Lysine oxidase activity of l-AAO/MOG was increased in a p-chloromercuribenzoate (p-CMB) concentration-dependent manner to a final level that was five fold higher than that of the non-treated enzyme. In order to explain the effects of modification by the sulfhydryl reagent, saturation mutagenesis studies were carried out on five cysteine residues, and we succeeded in identifying l-AAO/MOG C254I mutant enzyme, which showed five-times higher specific activity of oxidase activity than that of wild type. The monooxygenase activity shown by the C254I variant was decreased significantly. Moreover, we also determined a high-resolution three-dimensional structure of l-AAO/MOG to provide a structural basis for its biochemical characteristics. The key residue for the activity conversion of l-AAO/MOG, Cys-254, is located near the aromatic cage (Trp-418, Phe-473, and Trp-516). Although the location of Cys-254 indicates that it is not directly involved in the substrate binding, the chemical modification by p-CMB or C254I mutation would have a significant impact on the substrate binding via the side chain of Trp-516. It is suggested that a slight difference of the binding position of a substrate can dictate the activity of this type of enzyme as oxidase or monooxygenase.
 
Mutational and crystallographic analysis of l-amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813: Interconversion between oxidase and monooxygenase activities.,Matsui D, Im DH, Sugawara A, Fukuta Y, Fushinobu S, Isobe K, Asano Y FEBS Open Bio. 2014 Feb 7;4:220-8. doi: 10.1016/j.fob.2014.02.002. eCollection, 2014. PMID:24693490<ref>PMID:24693490</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3we0" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]]
*[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Achromobacter georgiopolitanum]]
[[Category: L-amino-acid oxidase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Asano, Y]]
[[Category: Pseudomonas sp]]
[[Category: Fukuta, Y]]
[[Category: Asano Y]]
[[Category: Fushinobu, S]]
[[Category: Fukuta Y]]
[[Category: Im, D H]]
[[Category: Fushinobu S]]
[[Category: Isobe, K]]
[[Category: Im DH]]
[[Category: Matsui, D]]
[[Category: Isobe K]]
[[Category: Flavin-containing monoamine oxidase family]]
[[Category: Matsui D]]
[[Category: Oxidoreductase]]
[[Category: Rossmann fold]]

Latest revision as of 11:44, 20 March 2024

L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813L-Amino acid oxidase/monooxygenase from Pseudomonas sp. AIU 813

Structural highlights

3we0 is a 2 chain structure with sequence from Pseudomonas sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B3IVI6_PSEPU

See Also

3we0, resolution 1.90Å

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