4tm8
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tm8]] 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=4TM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TM8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4tm8]] 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=4TM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TM8 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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]] 1.81Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4tm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tm8 OCA], [https://pdbe.org/4tm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tm8 RCSB], [https://www.ebi.ac.uk/pdbsum/4tm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tm8 ProSAT]</span></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=4tm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tm8 OCA], [https://pdbe.org/4tm8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tm8 RCSB], [https://www.ebi.ac.uk/pdbsum/4tm8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tm8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/A0QWX6_MYCS2 A0QWX6_MYCS2] | [https://www.uniprot.org/uniprot/A0QWX6_MYCS2 A0QWX6_MYCS2] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4tm8" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of 6-phosphogluconolactonase from Mycobacterium smegmatis N131D mutant
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