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==Crystal structure of 6-phosphogluconolactonase from Mycobacterium smegmatis N131D mutant soaked with CuSO4==
==Crystal structure of 6-phosphogluconolactonase from Mycobacterium smegmatis N131D mutant soaked with CuSO4==
<StructureSection load='4tm7' size='340' side='right' caption='[[4tm7]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
<StructureSection load='4tm7' size='340' side='right'caption='[[4tm7]], [[Resolution|resolution]] 1.39&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4tm7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TM7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TM7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4tm7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TM7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TM7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.39&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tm8|4tm8]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pgl, MSMEG_3099, MSMEI_3021 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tm7 OCA], [https://pdbe.org/4tm7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tm7 RCSB], [https://www.ebi.ac.uk/pdbsum/4tm7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tm7 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/6-phosphogluconolactonase 6-phosphogluconolactonase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.31 3.1.1.31] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tm7 OCA], [http://pdbe.org/4tm7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tm7 RCSB], [http://www.ebi.ac.uk/pdbsum/4tm7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tm7 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/A0QWX6_MYCS2 A0QWX6_MYCS2]
As an alternative to Darwinian evolution relying on catalytic promiscuity, a protein may acquire auxiliary function upon metal binding, thus providing it with a novel catalytic machinery. Here we show that addition of cupric ions to a 6-phosphogluconolactonase 6-PGLac bearing a putative metal binding site leads to the emergence of peroxidase activity (kcat 7.8 x 10(-2) s(-1), KM 1.1 x 10(-5) M). Both X-ray crystallographic and EPR data of the copper-loaded enzyme Cu.6-PGLac reveal a bis-histidine coordination site, located within a shallow binding pocket capable of accommodating the o-dianisidine substrate.
 
Enzyme repurposing of a hydrolase as an emergent peroxidase upon metal binding.,Fujieda N, Schatti J, Stuttfeld E, Ohkubo K, Maier T, Fukuzumi S, Ward TR Chem Sci. 2015 Jul 1;6(7):4060-4065. doi: 10.1039/c5sc01065a. Epub 2015 May 7. PMID:29218172<ref>PMID:29218172</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4tm7" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 6-phosphogluconolactonase]]
[[Category: Large Structures]]
[[Category: Mycs2]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: Fujieda, N]]
[[Category: Fujieda N]]
[[Category: Maier, T]]
[[Category: Maier T]]
[[Category: Stuttfeld, E]]
[[Category: Stuttfeld E]]
[[Category: Hydrolase]]
[[Category: Rossmann fold]]

Latest revision as of 09:00, 20 March 2024

Crystal structure of 6-phosphogluconolactonase from Mycobacterium smegmatis N131D mutant soaked with CuSO4

4tm7, resolution 1.39Å

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