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| | <StructureSection load='5ufv' size='340' side='right'caption='[[5ufv]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='5ufv' size='340' side='right'caption='[[5ufv]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ufv]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Myctt Myctt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UFV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5UFV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ufv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermothelomyces_thermophilus_ATCC_42464 Thermothelomyces thermophilus ATCC 42464]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5UFV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5UFV FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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]] 2.45Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HIC:4-METHYL-HISTIDINE'>HIC</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYCTH_92668 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573729 MYCTT])</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=5ufv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ufv OCA], [https://pdbe.org/5ufv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ufv RCSB], [https://www.ebi.ac.uk/pdbsum/5ufv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ufv ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ufv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ufv OCA], [http://pdbe.org/5ufv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ufv RCSB], [http://www.ebi.ac.uk/pdbsum/5ufv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ufv ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G2QAB5_MYCTT G2QAB5_MYCTT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Myctt]] | + | [[Category: Thermothelomyces thermophilus ATCC 42464]] |
| - | [[Category: Deller, M C]] | + | [[Category: Deller MC]] |
| - | [[Category: Marletta, M A]] | + | [[Category: Marletta MA]] |
| - | [[Category: Span, E A]] | + | [[Category: Span EA]] |
| - | [[Category: Biocatalysis]]
| + | |
| - | [[Category: Copper protein]]
| + | |
| - | [[Category: Fungal protein]]
| + | |
| - | [[Category: Hydrolase-oxidoreductase complex]]
| + | |
| - | [[Category: Oxidation-reduction]]
| + | |
| - | [[Category: Oxygen]]
| + | |
| Structural highlights
Function
G2QAB5_MYCTT
Publication Abstract from PubMed
Polysaccharide monooxygenases (PMOs) are secreted metalloenzymes that catalyze the oxidative degradation of polysaccharides in a copper-, oxygen-, and reductant-dependent manner. Cellulose-active fungal PMOs degrade cellulosic substrates to be utilized as a carbon source for fungal growth. To gain insight into the PMO mechanism, the role of conserved residues in the copper coordination sphere was investigated. Here, we report active-site hydrogen-bonding motifs in the secondary copper coordination sphere of MtPMO3*, a C1-oxidizing PMO from the ascomycete fungus Myceliophthora thermophila. A series of point substitutions that disrupt this conserved network are used to interrogate its function. Activity assays, in conjunction with EPR spectroscopy, demonstrate that residues H161 and Q167 are involved in stabilizing bound oxygen, and H161 appears to play a role in proton transfer. Additionally, Q167 increases the ligand donor strength of Y169 to the copper via a hydrogen-bonding interaction. Altogether, H161 and Q167 are important for oxygen activation, and the results are suggestive of a copper-oxyl active intermediate.
The Role of the Secondary Coordination Sphere in a Fungal Polysaccharide Monooxygenase.,Span EA, Suess DL, Deller MC, Britt RD, Marletta MA ACS Chem Biol. 2017 Mar 3. doi: 10.1021/acschembio.7b00016. PMID:28257189[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Span EA, Suess DL, Deller MC, Britt RD, Marletta MA. The Role of the Secondary Coordination Sphere in a Fungal Polysaccharide Monooxygenase. ACS Chem Biol. 2017 Mar 3. doi: 10.1021/acschembio.7b00016. PMID:28257189 doi:http://dx.doi.org/10.1021/acschembio.7b00016
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