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'''Unreleased structure'''


The entry 5ts5 is ON HOLD  until Paper Publication
==Crystal structure of L-amino acid oxidase from Bothrops atrox==
<StructureSection load='5ts5' size='340' side='right'caption='[[5ts5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ts5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bothrops_atrox Bothrops atrox]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TS5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TS5 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]] 2.3&#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=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=5ts5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ts5 OCA], [https://pdbe.org/5ts5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ts5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ts5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ts5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/OXLA_BOTAT OXLA_BOTAT] Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:18804547). Shows high catalytic activity against L-Met, L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile (PubMed:18804547). Shows no or weak activity on L-Cys, L-Val, L-Gln, L-Thr, L-Ser, L-Lys, L-Arg, L-Asn, L-Glu, L-Gly, L-Pro, L-Asp and L-His (PubMed:18804547). Induces platelet aggregation in platelet-rich plasma, probably due to hydrogen peroxide production, since catalase inhibits aggregation effect (PubMed:18804547). Induces moderate mouse paw edema (PubMed:18804547). Induces apoptosis and shows cytotoxicity against several cancer cell lines, which is inhibited by catalase (PubMed:18804547, PubMed:21300133). Shows hemolytic activity and antibacterial activities against both Gram-positive and Gram-negative bacteria (PubMed:21300133). Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (PubMed:21300133). Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage (with 50 ug of enzyme) (PubMed:18804547).<ref>PMID:18804547</ref> <ref>PMID:21300133</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
L-amino acid oxidases (LAAOs) are dimeric flavoproteins that catalyze the deamination of L-amino acid to alpha-keto acid, producing ammonia and hydrogen peroxide. In this study, we report the crystal structure and molecular dynamics simulations of LAAO from the venom of Bothrops atrox (BatroxLAAO). BatroxLAAO presents several biological and pharmacological properties with promising biomedical applications. BatroxLAAO structure contains the highly conserved structural pattern of LAAOs comprising a FAD-binding domain, substrate-binding domain and helical domain, and a dimeric arrangement that can be stabilized by zinc. Also, molecular dynamics results show an asymmetric behavior, and a direct communication between FAD- and substrate-binding domains of counterpart subunits. These findings shed light on the structural role of dimerization to catalytic mechanism of SV-LAAOs.


Authors: Feliciano, P.R., Nonato, M.C.
Crystal structure and molecular dynamics studies of L-amino acid oxidase from Bothrops atrox.,Feliciano PR, Rustiguel JK, Soares RO, Sampaio SV, Cristina Nonato M Toxicon. 2017 Mar 15;128:50-59. doi: 10.1016/j.toxicon.2017.01.017. Epub 2017 Jan, 27. PMID:28137621<ref>PMID:28137621</ref>


Description: Crystal structure of L-amino acid oxidase from Bothrops atrox
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Nonato, M.C]]
<div class="pdbe-citations 5ts5" style="background-color:#fffaf0;"></div>
[[Category: Feliciano, P.R]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bothrops atrox]]
[[Category: Large Structures]]
[[Category: Feliciano PR]]
[[Category: Nonato MC]]

Latest revision as of 12:14, 25 October 2023

Crystal structure of L-amino acid oxidase from Bothrops atroxCrystal structure of L-amino acid oxidase from Bothrops atrox

Structural highlights

5ts5 is a 4 chain structure with sequence from Bothrops atrox. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:, , , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

OXLA_BOTAT Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (PubMed:18804547). Shows high catalytic activity against L-Met, L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile (PubMed:18804547). Shows no or weak activity on L-Cys, L-Val, L-Gln, L-Thr, L-Ser, L-Lys, L-Arg, L-Asn, L-Glu, L-Gly, L-Pro, L-Asp and L-His (PubMed:18804547). Induces platelet aggregation in platelet-rich plasma, probably due to hydrogen peroxide production, since catalase inhibits aggregation effect (PubMed:18804547). Induces moderate mouse paw edema (PubMed:18804547). Induces apoptosis and shows cytotoxicity against several cancer cell lines, which is inhibited by catalase (PubMed:18804547, PubMed:21300133). Shows hemolytic activity and antibacterial activities against both Gram-positive and Gram-negative bacteria (PubMed:21300133). Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production (PubMed:21300133). Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage (with 50 ug of enzyme) (PubMed:18804547).[1] [2]

Publication Abstract from PubMed

L-amino acid oxidases (LAAOs) are dimeric flavoproteins that catalyze the deamination of L-amino acid to alpha-keto acid, producing ammonia and hydrogen peroxide. In this study, we report the crystal structure and molecular dynamics simulations of LAAO from the venom of Bothrops atrox (BatroxLAAO). BatroxLAAO presents several biological and pharmacological properties with promising biomedical applications. BatroxLAAO structure contains the highly conserved structural pattern of LAAOs comprising a FAD-binding domain, substrate-binding domain and helical domain, and a dimeric arrangement that can be stabilized by zinc. Also, molecular dynamics results show an asymmetric behavior, and a direct communication between FAD- and substrate-binding domains of counterpart subunits. These findings shed light on the structural role of dimerization to catalytic mechanism of SV-LAAOs.

Crystal structure and molecular dynamics studies of L-amino acid oxidase from Bothrops atrox.,Feliciano PR, Rustiguel JK, Soares RO, Sampaio SV, Cristina Nonato M Toxicon. 2017 Mar 15;128:50-59. doi: 10.1016/j.toxicon.2017.01.017. Epub 2017 Jan, 27. PMID:28137621[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Alves RM, Antonucci GA, Paiva HH, Cintra AC, Franco JJ, Mendonca-Franqueiro EP, Dorta DJ, Giglio JR, Rosa JC, Fuly AL, Dias-Baruffi M, Soares AM, Sampaio SV. Evidence of caspase-mediated apoptosis induced by l-amino acid oxidase isolated from Bothrops atrox snake venom. Comp Biochem Physiol A Mol Integr Physiol. 2008 Dec;151(4):542-50. doi: , 10.1016/j.cbpa.2008.07.007. Epub 2008 Jul 11. PMID:18804547 doi:http://dx.doi.org/10.1016/j.cbpa.2008.07.007
  2. ↑ de Melo Alves Paiva R, de Freitas Figueiredo R, Antonucci GA, Paiva HH, de Lourdes Pires Bianchi M, Rodrigues KC, Lucarini R, Caetano RC, Linhari Rodrigues Pietro RC, Martins CH, de Albuquerque S, Sampaio SV. Cell cycle arrest evidence, parasiticidal and bactericidal properties induced by L-amino acid oxidase from Bothrops atrox snake venom. Biochimie. 2011 May;93(5):941-7. doi: 10.1016/j.biochi.2011.01.009. Epub 2011 Feb , 12. PMID:21300133 doi:http://dx.doi.org/10.1016/j.biochi.2011.01.009
  3. ↑ Feliciano PR, Rustiguel JK, Soares RO, Sampaio SV, Cristina Nonato M. Crystal structure and molecular dynamics studies of L-amino acid oxidase from Bothrops atrox. Toxicon. 2017 Mar 15;128:50-59. doi: 10.1016/j.toxicon.2017.01.017. Epub 2017 Jan, 27. PMID:28137621 doi:http://dx.doi.org/10.1016/j.toxicon.2017.01.017

5ts5, resolution 2.30Å

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