6fyq
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of a new transaminase from the marine bacterium Virgibacillus== |
| + | <StructureSection load='6fyq' size='340' side='right' caption='[[6fyq]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6fyq]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FYQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FYQ FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-alanine--pyruvate_transaminase Beta-alanine--pyruvate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.18 2.6.1.18] </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=6fyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fyq OCA], [http://pdbe.org/6fyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fyq RCSB], [http://www.ebi.ac.uk/pdbsum/6fyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fyq ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | A new transaminase (VbTA) was identified from the genome of the halotolerant marine bacterium Virgibacillus 21D. Following heterologous expression in Escherichia coli, it was located entirely in the insoluble fraction. After a single mutation, identified via sequence homology analyses, the VbTA T16F mutant was successfully expressed in soluble form and characterised. VbTA T16F showed high stability towards polar organic solvents and salt exposure, accepting mainly hydrophobic aromatic amine and carbonyl substrates. The 2.0 A resolution crystal structure of VbTA T16F is here reported, and together with computational calculations, revealed that this mutation is crucial for correct dimerisation and thus correct folding, leading to soluble protein expression. | ||
| - | + | Strategic single point mutation yields a solvent- and salt-stable transaminase from Virgibacillus sp. in soluble form.,Guidi B, Planchestainer M, Contente ML, Laurenzi T, Eberini I, Gourlay LJ, Romano D, Paradisi F, Molinari F Sci Rep. 2018 Nov 6;8(1):16441. doi: 10.1038/s41598-018-34434-3. PMID:30401905<ref>PMID:30401905</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6fyq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beta-alanine--pyruvate transaminase]] | ||
| + | [[Category: Gourlay, L J]] | ||
| + | [[Category: Omega-amino acid-pyruvate aminotransferase]] | ||
| + | [[Category: Transferase]] | ||
| + | [[Category: Virgibacillus pantothenticus]] | ||
Current revision
The crystal structure of a new transaminase from the marine bacterium Virgibacillus
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