1reo

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(New page: 200px<br /><applet load="1reo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1reo, resolution 2.31&Aring;" /> '''L-amino acid oxidase...)
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[[Image:1reo.jpg|left|200px]]<br /><applet load="1reo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1reo, resolution 2.31&Aring;" />
 
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'''L-amino acid oxidase from Agkistrodon halys pallas'''<br />
 
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==Overview==
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==L-amino acid oxidase from Agkistrodon halys pallas==
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A snake-venom protein named AHP-LAAO has been purified from Agkistrodon, halys pallas venom using four-stage chromatography. AHP-LAAO is a novel, member of the snake-venom L-amino-acid oxidase family. Its amino-acid, sequence shows high homology to other members of this family. For, L-leucine, the values of k(cat) and K(M) are 31.1 s(-1) and 0.25 mM, respectively. The molecular weight of AHP-LAAO is about 60.7 kDa as, determined by MALDI-TOF mass spectrometry. AHP-LAAO can also induce, apoptosis of cultured Hela cells. Two sets of diffraction data with, similar resolution limits (about 2.5 A) were collected independently at, MacCHESS (Cornell High Energy Synchrotron Source, USA) and IHEP (Institute, of High Energy Physics, Beijing, China). The crystals belong to space, group I2(1)3, with unit-cell parameter a = 169.31 A, corresponding to one, molecule in the asymmetric unit and a volume-to-weight ratio of 3.33 A(3), Da(-1). The final structural model is similar to that of L-amino-acid, oxidase from Calloselasma rhodostoma venom.
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<StructureSection load='1reo' size='340' side='right'caption='[[1reo]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1reo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gloydius_halys Gloydius halys]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1REO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1REO FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.31&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1reo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1reo OCA], [https://pdbe.org/1reo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1reo RCSB], [https://www.ebi.ac.uk/pdbsum/1reo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1reo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/OXLA_GLOHA OXLA_GLOHA] 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. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, antibacterial and antiparasitic activities, as well as regulation of platelet aggregation. Its effect on platelets is controversial, since it either induces aggregation or inhibits agonist-induced aggregation. These different effects are probably due to different experimental conditions (By similarity). This protein induces apoptosis of cultured HeLa cells.<ref>PMID:15103157</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/re/1reo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1reo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A snake-venom protein named AHP-LAAO has been purified from Agkistrodon halys pallas venom using four-stage chromatography. AHP-LAAO is a novel member of the snake-venom L-amino-acid oxidase family. Its amino-acid sequence shows high homology to other members of this family. For L-leucine, the values of k(cat) and K(M) are 31.1 s(-1) and 0.25 mM, respectively. The molecular weight of AHP-LAAO is about 60.7 kDa as determined by MALDI-TOF mass spectrometry. AHP-LAAO can also induce apoptosis of cultured Hela cells. Two sets of diffraction data with similar resolution limits (about 2.5 A) were collected independently at MacCHESS (Cornell High Energy Synchrotron Source, USA) and IHEP (Institute of High Energy Physics, Beijing, China). The crystals belong to space group I2(1)3, with unit-cell parameter a = 169.31 A, corresponding to one molecule in the asymmetric unit and a volume-to-weight ratio of 3.33 A(3) Da(-1). The final structural model is similar to that of L-amino-acid oxidase from Calloselasma rhodostoma venom.
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==About this Structure==
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Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom.,Zhang H, Teng M, Niu L, Wang Y, Wang Y, Liu Q, Huang Q, Hao Q, Dong Y, Liu P Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):974-7. Epub 2004, Apr 21. PMID:15103157<ref>PMID:15103157</ref>
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1REO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gloydius_halys Gloydius halys] with NAG, NDG, CIT and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/L-amino-acid_oxidase L-amino-acid oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.2 1.4.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1REO OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Purification, partial characterization, crystallization and structural determination of AHP-LAAO, a novel L-amino-acid oxidase with cell apoptosis-inducing activity from Agkistrodon halys pallas venom., Zhang H, Teng M, Niu L, Wang Y, Wang Y, Liu Q, Huang Q, Hao Q, Dong Y, Liu P, Acta Crystallogr D Biol Crystallogr. 2004 May;60(Pt 5):974-7. Epub 2004, Apr 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15103157 15103157]
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</div>
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[[Category: Gloydius halys]]
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<div class="pdbe-citations 1reo" style="background-color:#fffaf0;"></div>
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[[Category: L-amino-acid oxidase]]
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[[Category: Single protein]]
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[[Category: Dong, Y.]]
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[[Category: Hao, Q.]]
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[[Category: Huang, Q.]]
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[[Category: Liu, P.]]
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[[Category: Liu, Q.]]
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[[Category: Niu, L.]]
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[[Category: Teng, M.]]
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[[Category: Wang, Y.]]
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[[Category: Zhang, H.]]
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[[Category: CIT]]
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[[Category: FAD]]
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[[Category: NAG]]
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[[Category: NDG]]
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[[Category: l-amino acid oxidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:31:51 2007''
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==See Also==
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*[[Amino acid oxidase 3D structures|Amino acid oxidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gloydius halys]]
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[[Category: Large Structures]]
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[[Category: Dong Y]]
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[[Category: Hao Q]]
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[[Category: Huang Q]]
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[[Category: Liu P]]
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[[Category: Liu Q]]
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[[Category: Niu L]]
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[[Category: Teng M]]
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[[Category: Wang Y]]
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[[Category: Zhang H]]

Current revision

L-amino acid oxidase from Agkistrodon halys pallas

PDB ID 1reo

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