4pva
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4pva is ON HOLD Authors: Nocek, B., Kaur, A.P., Xu, X., Cui, H., Savchenko, A. Description: Crystal structure of GH62 hydrolase from thermophilic f...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of GH62 hydrolase from thermophilic fungus Scytalidium thermophilum== | |
| + | <StructureSection load='4pva' size='340' side='right'caption='[[4pva]], [[Resolution|resolution]] 1.23Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4pva]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycothermus_thermophilus Mycothermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PVA FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.23Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4pva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pva OCA], [https://pdbe.org/4pva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pva RCSB], [https://www.ebi.ac.uk/pdbsum/4pva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pva ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A059U759_9PEZI A0A059U759_9PEZI] Alpha-L-arabinofuranosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Releases L-arabinose from arabinoxylan.[ARBA:ARBA00025637][RuleBase:RU368117] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The genome of the thermophilic fungus Scytalidium thermophilum (strain CBS 625.91) harbours a wide range of genes involved in carbohydrate degradation, including three genes, abf62A, abf62B and abf62C, predicted to encode glycoside hydrolase family 62 (GH62) enzymes. Transcriptome analysis showed that only abf62A and abf62C are actively expressed during growth on diverse substrates including straws from barley, alfalfa, triticale and canola. The abf62A and abf62C genes were expressed in Escherichia coli and the resulting recombinant proteins were characterized. Calcium-free crystal structures of Abf62C in apo and xylotriose bound forms were determined to 1.23 and 1.48 A resolution respectively. Site-directed mutagenesis confirmed Asp55, Asp171 and Glu230 as catalytic triad residues, and revealed the critical role of non-catalytic residues Asp194, Trp229 and Tyr338 in positioning the scissile alpha-L-arabinofuranoside bond at the catalytic site. Further, the +2R substrate-binding site residues Tyr168 and Asn339, as well as the +2NR residue Tyr226, are involved in accommodating long-chain xylan polymers. Overall, our structural and functional analysis highlights characteristic differences between Abf62A and Abf62C, which represent divergent subgroups in the GH62 family. | ||
| - | + | Functional and structural diversity in GH62 alpha-L-arabinofuranosidases from the thermophilic fungus Scytalidium thermophilum.,Kaur AP, Nocek BP, Xu X, Lowden MJ, Leyva JF, Stogios PJ, Cui H, Di Leo R, Powlowski J, Tsang A, Savchenko A Microb Biotechnol. 2014 Sep 29. doi: 10.1111/1751-7915.12168. PMID:25267315<ref>PMID:25267315</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4pva" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mycothermus thermophilus]] | ||
| + | [[Category: Cui H]] | ||
| + | [[Category: Kaur AP]] | ||
| + | [[Category: Nocek B]] | ||
| + | [[Category: Savchenko A]] | ||
| + | [[Category: Xu X]] | ||
Current revision
Crystal structure of GH62 hydrolase from thermophilic fungus Scytalidium thermophilum
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