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2btw

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[[Image:2btw.gif|left|200px]]<br />
 
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<applet load="2btw" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2btw, resolution 2.00&Aring;" />
 
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'''CRYSTAL STRUCTURE OF ALR0975'''<br />
 
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==Overview==
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==Crystal structure of Alr0975==
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Phytochelatin synthase (PCS) is a key enzyme for heavy-metal, detoxification in plants. PCS catalyzes the production of glutathione, (GSH)-derived peptides (called phytochelatins or PCs) that bind, heavy-metal ions before vacuolar sequestration. The enzyme can also, hydrolyze GSH and GS-conjugated xenobiotics. In the cyanobacterium Nostoc, the enzyme (NsPCS) contains only the catalytic domain of the eukaryotic, synthase and can act as a GSH hydrolase and weakly as a peptide ligase., The crystal structure of NsPCS in its native form solved at a 2.0-A, resolution shows that NsPCS is a dimer that belongs to the papain, superfamily of cysteine proteases, with a conserved catalytic machinery., Moreover, the structure of the protein solved as a complex with GSH at a, 1.4-A resolution reveals a gamma-glutamyl cysteine acyl-enzyme, intermediate stabilized in a cavity of the protein adjacent to a second, putative GSH binding site. GSH hydrolase and PCS activities of the enzyme, are discussed in the light of both structures.
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<StructureSection load='2btw' size='340' side='right'caption='[[2btw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2btw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BTW 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&#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=MSE:SELENOMETHIONINE'>MSE</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=2btw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btw OCA], [https://pdbe.org/2btw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2btw RCSB], [https://www.ebi.ac.uk/pdbsum/2btw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2btw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8YY76_NOSS1 Q8YY76_NOSS1]
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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/bt/2btw_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=2btw 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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Phytochelatin synthase (PCS) is a key enzyme for heavy-metal detoxification in plants. PCS catalyzes the production of glutathione (GSH)-derived peptides (called phytochelatins or PCs) that bind heavy-metal ions before vacuolar sequestration. The enzyme can also hydrolyze GSH and GS-conjugated xenobiotics. In the cyanobacterium Nostoc, the enzyme (NsPCS) contains only the catalytic domain of the eukaryotic synthase and can act as a GSH hydrolase and weakly as a peptide ligase. The crystal structure of NsPCS in its native form solved at a 2.0-A resolution shows that NsPCS is a dimer that belongs to the papain superfamily of cysteine proteases, with a conserved catalytic machinery. Moreover, the structure of the protein solved as a complex with GSH at a 1.4-A resolution reveals a gamma-glutamyl cysteine acyl-enzyme intermediate stabilized in a cavity of the protein adjacent to a second putative GSH binding site. GSH hydrolase and PCS activities of the enzyme are discussed in the light of both structures.
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==About this Structure==
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A papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis.,Vivares D, Arnoux P, Pignol D Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18848-53. Epub 2005 Dec 9. PMID:16339904<ref>PMID:16339904</ref>
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2BTW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Glutathione_gamma-glutamylcysteinyltransferase Glutathione gamma-glutamylcysteinyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.15 2.3.2.15] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BTW 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 papain-like enzyme at work: native and acyl-enzyme intermediate structures in phytochelatin synthesis., Vivares D, Arnoux P, Pignol D, Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18848-53. Epub 2005 Dec 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16339904 16339904]
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</div>
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[[Category: Anabaena sp.]]
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<div class="pdbe-citations 2btw" style="background-color:#fffaf0;"></div>
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[[Category: Glutathione gamma-glutamylcysteinyltransferase]]
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== References ==
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[[Category: Protein complex]]
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<references/>
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[[Category: Arnoux, P.]]
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__TOC__
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[[Category: Pignol, D.]]
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</StructureSection>
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[[Category: Vivares, D.]]
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[[Category: Large Structures]]
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[[Category: CA]]
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[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
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[[Category: alr0975]]
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[[Category: Arnoux P]]
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[[Category: cysteine protease]]
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[[Category: Pignol D]]
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[[Category: glutathione metabolism]]
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[[Category: Vivares D]]
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[[Category: nostoc]]
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[[Category: pcs]]
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[[Category: phytochelatin synthase]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:48:33 2007''
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Current revision

Crystal structure of Alr0975

PDB ID 2btw

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