1pe9

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(New page: 200px<br /><applet load="1pe9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pe9, resolution 1.60&Aring;" /> '''MUTATIONS IN THE T1....)
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[[Image:1pe9.jpg|left|200px]]<br /><applet load="1pe9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pe9, resolution 1.60&Aring;" />
 
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'''MUTATIONS IN THE T1.5 LOOP OF PECTATE LYASE A'''<br />
 
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==Overview==
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==MUTATIONS IN THE T1.5 LOOP OF PECTATE LYASE A==
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Pectate lyase A (PelA) is a pectate-degrading enzyme secreted by plant, pathogens. PelA from Erwinia chrysanthemi has 61% amino-acid identity and, a conserved structural similarity to pectate lyase E (PelE). Although, similar in structure and sequence, the enzymatic characteristics of PelA, differ from those for PelE. A structural alignment of PelA and PelE, reveals differences in the T1.5 loop. The sequence of the T1.5 loop in, PelA was mutated to the homologous sequence in PelE. The crystal structure, of the PelA T1.5 mutant has been solved to 1.6 and 2.9 A resolution. The, enzymatic and structural properties of the T1.5 mutant are discussed.
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<StructureSection load='1pe9' size='340' side='right'caption='[[1pe9]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1pe9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_chrysanthemi Dickeya chrysanthemi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PE9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PE9 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]] 1.6&#8491;</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=1pe9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pe9 OCA], [https://pdbe.org/1pe9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pe9 RCSB], [https://www.ebi.ac.uk/pdbsum/1pe9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pe9 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PLYA_DICCH PLYA_DICCH] Involved in maceration and soft-rotting of plant tissue.
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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/pe/1pe9_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=1pe9 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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Pectate lyase A (PelA) is a pectate-degrading enzyme secreted by plant pathogens. PelA from Erwinia chrysanthemi has 61% amino-acid identity and a conserved structural similarity to pectate lyase E (PelE). Although similar in structure and sequence, the enzymatic characteristics of PelA differ from those for PelE. A structural alignment of PelA and PelE reveals differences in the T1.5 loop. The sequence of the T1.5 loop in PelA was mutated to the homologous sequence in PelE. The crystal structure of the PelA T1.5 mutant has been solved to 1.6 and 2.9 A resolution. The enzymatic and structural properties of the T1.5 mutant are discussed.
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==About this Structure==
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Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16.,Dehdashti SJ, Doan CN, Chao KL, Yoder MD Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1339-42. Epub 2003, Jun 27. PMID:12832805<ref>PMID:12832805</ref>
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1PE9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Erwinia_chrysanthemi Erwinia chrysanthemi]. Active as [http://en.wikipedia.org/wiki/Pectate_lyase Pectate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PE9 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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Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16., Dehdashti SJ, Doan CN, Chao KL, Yoder MD, Acta Crystallogr D Biol Crystallogr. 2003 Jul;59(Pt 7):1339-42. Epub 2003, Jun 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12832805 12832805]
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</div>
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[[Category: Erwinia chrysanthemi]]
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<div class="pdbe-citations 1pe9" style="background-color:#fffaf0;"></div>
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[[Category: Pectate lyase]]
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== References ==
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[[Category: Single protein]]
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<references/>
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[[Category: Chao, K.L.]]
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__TOC__
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[[Category: Dehdashti, S.J.]]
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</StructureSection>
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[[Category: Doan, C.N.]]
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[[Category: Dickeya chrysanthemi]]
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[[Category: Yoder, M.D.]]
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[[Category: Large Structures]]
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[[Category: parallel beta helix]]
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[[Category: Chao KL]]
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[[Category: Dehdashti SJ]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:44:03 2007''
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[[Category: Doan CN]]
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[[Category: Yoder MD]]

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MUTATIONS IN THE T1.5 LOOP OF PECTATE LYASE A

PDB ID 1pe9

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