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4gbo
From Proteopedia
(Difference between revisions)
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==Structure of T.fusca E7== | ==Structure of T.fusca E7== | ||
| - | <StructureSection load='4gbo' size='340' side='right' caption='[[4gbo]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4gbo' size='340' side='right'caption='[[4gbo]], [[Resolution|resolution]] 2.00Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4gbo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GBO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GBO FirstGlance]. <br> | <table><tr><td colspan='2'>[[4gbo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermonospora_fusca"_henssen_1957 "thermonospora fusca" henssen 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GBO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GBO FirstGlance]. <br> | ||
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<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=4gbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gbo OCA], [http://pdbe.org/4gbo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gbo RCSB], [http://www.ebi.ac.uk/pdbsum/4gbo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gbo 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=4gbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gbo OCA], [http://pdbe.org/4gbo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gbo RCSB], [http://www.ebi.ac.uk/pdbsum/4gbo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gbo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Background: Auxiliary activity (AA) enzymes are produced by numerous bacterial and fungal species to assist in the degradation of biomass. These enzymes are abundant but have yet to be fully characterized. Here, we report the X-ray structure of Thermobifida fusca AA10A (TfAA10A), investigate mutational characterization of key surface residues near its active site, and explore the importance of the various domains of Thermobifida fusca AA10B (TfAA10B). The structure of TfAA10A is similar to other bacterial LPMOs (lytic polysaccharide monooxygenases), including signs of photo-reduction and a distorted active site, with mixed features showing both type I and II copper coordination. The point mutation experiments of TfAA10A show that Trp82 and Asn83 are needed for binding, but only Trp82 affects activity. The TfAA10B domain truncation mutants reveal that CBM2 is crucial for the binding of substrate, but that the X1 module does not affect binding or activity. Results: In TfAA10A, Trp82 and Asn83 are needed for binding, but only Trp82 affects activity. The TfAA10B domain truncation mutants reveal that CBM2 is crucial for substrate binding, but that the X1 module does not affect binding or activity. The structure of TfAA10A is similar to other bacterial lytic polysaccharide monooxygenases with mixed features showing both type I and II copper coordination. Conclusions: The role of LPMOs and the variability of abundance in genomes are not fully explored. LPMOs likely perform initial attacks into crystalline cellulose to allow larger processive cellulases to bind and attack, but the precise nature of their synergistic behavior remains to be definitively characterized. | ||
| + | |||
| + | Structure of a Thermobifida fusca lytic polysaccharide monooxygenase and mutagenesis of key residues.,Kruer-Zerhusen N, Alahuhta M, Lunin VV, Himmel ME, Bomble YJ, Wilson DB Biotechnol Biofuels. 2017 Nov 30;10:243. doi: 10.1186/s13068-017-0925-7., eCollection 2017. PMID:29213309<ref>PMID:29213309</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4gbo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Thermonospora fusca henssen 1957]] | [[Category: Thermonospora fusca henssen 1957]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Alahuhta, P M]] | [[Category: Alahuhta, P M]] | ||
[[Category: Lunin, V V]] | [[Category: Lunin, V V]] | ||
Revision as of 22:57, 5 June 2019
Structure of T.fusca E7
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