1tu5

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(New page: 200px<br /><applet load="1tu5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tu5, resolution 2.37&Aring;" /> '''Crystal structure of...)
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[[Image:1tu5.gif|left|200px]]<br /><applet load="1tu5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tu5, resolution 2.37&Aring;" />
 
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'''Crystal structure of bovine plasma copper-containing amine oxidase'''<br />
 
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==Overview==
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==Crystal structure of bovine plasma copper-containing amine oxidase==
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Copper-containing amine oxidase extracted from bovine serum (BSAO) was, crystallized and its three-dimensional structure at 2.37A resolution is, described. The biological unit of BSAO is a homodimer, formed by two, monomers related to each other by a non-crystallographic 2-fold axis. Each, monomer is composed of three domains, similar to those of other amine, oxidases from lower species. The two monomers are structurally equivalent, despite some minor differences at the two active sites. A large funnel, allows access of substrates to the active-site; another cavity, accessible, to the solvent, is also present between the two monomers; this second, cavity could allow the entrance of molecular oxygen necessary for the, oxidative reaction. Some sugar residues, bound to Asn, were still present, and visible in the electron density map, in spite of the exhaustive, deglycosylation necessary to grow the crystals. The comparison of the BSAO, structure with those of other resolved AO structures shows strong, dissimilarities in the architecture and charge distribution of the, cavities leading to the active-site, possibly explaining the differences, in substrate specificity.
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<StructureSection load='1tu5' size='340' side='right'caption='[[1tu5]], [[Resolution|resolution]] 2.37&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tu5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TU5 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]] 2.37&#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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</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=1tu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tu5 OCA], [https://pdbe.org/1tu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tu5 RCSB], [https://www.ebi.ac.uk/pdbsum/1tu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tu5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AOCX_BOVIN AOCX_BOVIN]
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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/tu/1tu5_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1tu5 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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Copper-containing amine oxidase extracted from bovine serum (BSAO) was crystallized and its three-dimensional structure at 2.37A resolution is described. The biological unit of BSAO is a homodimer, formed by two monomers related to each other by a non-crystallographic 2-fold axis. Each monomer is composed of three domains, similar to those of other amine oxidases from lower species. The two monomers are structurally equivalent, despite some minor differences at the two active sites. A large funnel allows access of substrates to the active-site; another cavity, accessible to the solvent, is also present between the two monomers; this second cavity could allow the entrance of molecular oxygen necessary for the oxidative reaction. Some sugar residues, bound to Asn, were still present and visible in the electron density map, in spite of the exhaustive deglycosylation necessary to grow the crystals. The comparison of the BSAO structure with those of other resolved AO structures shows strong dissimilarities in the architecture and charge distribution of the cavities leading to the active-site, possibly explaining the differences in substrate specificity.
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==About this Structure==
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Crystal structure of amine oxidase from bovine serum.,Lunelli M, Di Paolo ML, Biadene M, Calderone V, Battistutta R, Scarpa M, Rigo A, Zanotti G J Mol Biol. 2005 Mar 4;346(4):991-1004. Epub 2005 Jan 25. PMID:15701511<ref>PMID:15701511</ref>
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1TU5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with NAG, NDG, CU, CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TU5 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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Crystal structure of amine oxidase from bovine serum., Lunelli M, Di Paolo ML, Biadene M, Calderone V, Battistutta R, Scarpa M, Rigo A, Zanotti G, J Mol Biol. 2005 Mar 4;346(4):991-1004. Epub 2005 Jan 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15701511 15701511]
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</div>
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[[Category: Amine oxidase (copper-containing)]]
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<div class="pdbe-citations 1tu5" style="background-color:#fffaf0;"></div>
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[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Battistutta, R.]]
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[[Category: Biadene, M.]]
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[[Category: Calderone, V.]]
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[[Category: Lunelli, M.]]
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[[Category: Paolo, M.L.Di.]]
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[[Category: Rigo, A.]]
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[[Category: Scarpa, M.]]
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[[Category: Zanotti, G.]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: CU]]
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[[Category: NAG]]
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[[Category: NDG]]
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[[Category: amine oxidase]]
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[[Category: copper]]
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[[Category: oxidoreductase]]
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[[Category: quinoenzyme]]
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[[Category: tpq]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:35:35 2007''
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==See Also==
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*[[Copper amine oxidase 3D structures|Copper amine 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: Bos taurus]]
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[[Category: Large Structures]]
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[[Category: Battistutta R]]
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[[Category: Biadene M]]
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[[Category: Calderone V]]
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[[Category: Di Paolo ML]]
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[[Category: Lunelli M]]
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[[Category: Rigo A]]
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[[Category: Scarpa M]]
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[[Category: Zanotti G]]

Current revision

Crystal structure of bovine plasma copper-containing amine oxidase

PDB ID 1tu5

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