1it5

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(New page: 200px<br /><applet load="1it5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1it5" /> '''Solution structure of apo-type PLA2 from Str...)
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[[Image:1it5.gif|left|200px]]<br /><applet load="1it5" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1it5" />
 
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'''Solution structure of apo-type PLA2 from Streptomyces violaceruber A-2688.'''<br />
 
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==Overview==
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==Solution structure of apo-type PLA2 from Streptomyces violaceruber A-2688.==
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Until now, phospholipase A(2) (PLA(2); EC 3.1.14) has been found only from, eukaryotic sources. In the present study, we found a secreted PLA(2), which is produced by a soil bacterium, Streptomyces violaceoruber A-2688, demonstrating that the enzyme is the first phospholipase A(2) identified, in prokaryote. After characterization of the novel PLA(2), a gene encoding, the enzyme was cloned, sequenced, and overexpressed using a Streptomyces, host-vector system. The amino acid sequence showed that the prokaryotic, PLA(2) has only four cysteines and less homology to the eukaryotic ones, which have 12-16 cysteines. The solution structures of the prokaryotic, PLA(2), bound and unbound with calcium(II) ion, were determined by using, the NMR technique and structure calculation. The overall structure of the, S. violaceoruber PLA(2), which is composed of only five alpha-helices, is, completely different from those of eukaryotic PLA(2)s, which consist of, beta-sheets and alpha-helices. The structure of the calcium-binding domain, is obviously distinct from that without the ion; the ligands for the, calcium(II) ion are the two carboxylates of Asp(43) (monodentate) and, Asp(65) (bidentate), the carbonyl oxygen of Leu(44), and three water, molecules. A calcium-binding experiment showed that the calcium, dissociation constant ( approximately 5 mm) for the prokaryotic PLA(2) is, much larger than those of eukaryotic ones.
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<StructureSection load='1it5' size='340' side='right'caption='[[1it5]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1it5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_violaceoruber Streptomyces violaceoruber]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IT5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IT5 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">Solution NMR, 1 model</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=1it5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1it5 OCA], [https://pdbe.org/1it5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1it5 RCSB], [https://www.ebi.ac.uk/pdbsum/1it5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1it5 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q6UV28_STRVN Q6UV28_STRVN]
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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/it/1it5_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=1it5 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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Until now, phospholipase A(2) (PLA(2); EC 3.1.14) has been found only from eukaryotic sources. In the present study, we found a secreted PLA(2), which is produced by a soil bacterium, Streptomyces violaceoruber A-2688, demonstrating that the enzyme is the first phospholipase A(2) identified in prokaryote. After characterization of the novel PLA(2), a gene encoding the enzyme was cloned, sequenced, and overexpressed using a Streptomyces host-vector system. The amino acid sequence showed that the prokaryotic PLA(2) has only four cysteines and less homology to the eukaryotic ones, which have 12-16 cysteines. The solution structures of the prokaryotic PLA(2), bound and unbound with calcium(II) ion, were determined by using the NMR technique and structure calculation. The overall structure of the S. violaceoruber PLA(2), which is composed of only five alpha-helices, is completely different from those of eukaryotic PLA(2)s, which consist of beta-sheets and alpha-helices. The structure of the calcium-binding domain is obviously distinct from that without the ion; the ligands for the calcium(II) ion are the two carboxylates of Asp(43) (monodentate) and Asp(65) (bidentate), the carbonyl oxygen of Leu(44), and three water molecules. A calcium-binding experiment showed that the calcium dissociation constant ( approximately 5 mm) for the prokaryotic PLA(2) is much larger than those of eukaryotic ones.
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==About this Structure==
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A novel prokaryotic phospholipase A2. Characterization, gene cloning, and solution structure.,Sugiyama M, Ohtani K, Izuhara M, Koike T, Suzuki K, Imamura S, Misaki H J Biol Chem. 2002 May 31;277(22):20051-8. Epub 2002 Mar 15. PMID:11897786<ref>PMID:11897786</ref>
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1IT5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_violaceoruber Streptomyces violaceoruber]. Active as [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IT5 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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A novel prokaryotic phospholipase A2. Characterization, gene cloning, and solution structure., Sugiyama M, Ohtani K, Izuhara M, Koike T, Suzuki K, Imamura S, Misaki H, J Biol Chem. 2002 May 31;277(22):20051-8. Epub 2002 Mar 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11897786 11897786]
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</div>
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[[Category: Phospholipase A(2)]]
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<div class="pdbe-citations 1it5" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Streptomyces violaceoruber]]
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[[Category: Izuhara, M.]]
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[[Category: Koike, T.]]
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[[Category: Ohtani, K.]]
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[[Category: Sugiyama, M.]]
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[[Category: prokaryotic pla2]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 22:30:44 2007''
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==See Also==
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*[[Phospholipase A2 3D structures|Phospholipase A2 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: Large Structures]]
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[[Category: Streptomyces violaceoruber]]
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[[Category: Izuhara M]]
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[[Category: Koike T]]
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[[Category: Ohtani K]]
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[[Category: Sugiyama M]]

Current revision

Solution structure of apo-type PLA2 from Streptomyces violaceruber A-2688.

PDB ID 1it5

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