7qc8
From Proteopedia
(Difference between revisions)
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==HisF-C9A-D11E-V33A_L50H_I52H mutant in complex with Zn(II) from T. maritima== | ==HisF-C9A-D11E-V33A_L50H_I52H mutant in complex with Zn(II) from T. maritima== | ||
| - | <StructureSection load='7qc8' size='340' side='right'caption='[[7qc8]]' scene=''> | + | <StructureSection load='7qc8' size='340' side='right'caption='[[7qc8]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QC8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7qc8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QC8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QC8 FirstGlance]. <br> |
| - | </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=7qc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qc8 OCA], [https://pdbe.org/7qc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qc8 RCSB], [https://www.ebi.ac.uk/pdbsum/7qc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qc8 ProSAT]</span></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]] 1.8Å</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7qc8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qc8 OCA], [https://pdbe.org/7qc8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qc8 RCSB], [https://www.ebi.ac.uk/pdbsum/7qc8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qc8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/HIS6_THEMA HIS6_THEMA] IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Engineering non-native metal active sites into proteins using canonical amino acids offers many advantages but is hampered by significant challenges. The TIM barrel protein, imidazole glycerol phosphate synthase from the hyperthermophilic organism Thermotoga maritima (tHisF), is well-suited for the construction of artificial metalloenzymes by this approach. To this end, we have generated a tHisF variant (tHisF(EHH)) with a Glu/His/His motif for metal ion coordination. Crystal structures of Zn(II):tHisF(EHH) and Ni(II):tHisF(EHH) reveal that both metal ions bind to the engineered histidines. However, the two metals bind at distinct sites with different geometries, demonstrating the adaptability of tHisF. Only Zn(II) additionally ligates the Glu residue and adopts a tetrahedral geometry. The pseudo-octahedral Ni(II) site comprises the two His and a native Ser residue. Ni(II):tHisF(EHH) catalyzes the oxidative cleavage of the flavanols quercetin and myricetin, providing an unprecedented example of an artificial metalloprotein with quercetinase activity. | ||
| + | |||
| + | An artificial metalloprotein with metal-adaptive coordination sites and Ni-dependent quercetinase activity.,Beaumet M, Dose A, Brauer A, Mahy JP, Ghattas W, Groll M, Hess CR J Inorg Biochem. 2022 Jul 6;235:111914. doi: 10.1016/j.jinorgbio.2022.111914. PMID:35841720<ref>PMID:35841720</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7qc8" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Thermotoga maritima MSB8]] | ||
[[Category: Beaumet M]] | [[Category: Beaumet M]] | ||
[[Category: Braeuer A]] | [[Category: Braeuer A]] | ||
Current revision
HisF-C9A-D11E-V33A_L50H_I52H mutant in complex with Zn(II) from T. maritima
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Categories: Large Structures | Thermotoga maritima MSB8 | Beaumet M | Braeuer A | Dose A | Ghattas W | Groll M | Hess C | Mahy J
