4tm8
From Proteopedia
(Difference between revisions)
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<StructureSection load='4tm8' size='340' side='right' caption='[[4tm8]], [[Resolution|resolution]] 1.81Å' scene=''> | <StructureSection load='4tm8' size='340' side='right' caption='[[4tm8]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4tm8]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TM8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tm8]] 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=4TM8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TM8 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tm7|4tm7]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4tm7|4tm7]]</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='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='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=4tm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tm8 OCA], [http://pdbe.org/4tm8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tm8 RCSB], [http://www.ebi.ac.uk/pdbsum/4tm8 PDBsum], [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tm8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tm8 OCA], [http://pdbe.org/4tm8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tm8 RCSB], [http://www.ebi.ac.uk/pdbsum/4tm8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tm8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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. | ||
| + | |||
| + | 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®/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> | ||
[[Category: 6-phosphogluconolactonase]] | [[Category: 6-phosphogluconolactonase]] | ||
| + | [[Category: Mycs2]] | ||
[[Category: Fujieda, N]] | [[Category: Fujieda, N]] | ||
[[Category: Maier, T]] | [[Category: Maier, T]] | ||
Revision as of 20:21, 24 January 2018
Crystal structure of 6-phosphogluconolactonase from Mycobacterium smegmatis N131D mutant
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