View source for 6xgt


==Crystal structure of cyanase from the thermophilic fungus Thermomyces lanuginosus==
<StructureSection load='6xgt' size='340' side='right'caption='[[6xgt]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6xgt]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XGT 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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=6xgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xgt OCA], [https://pdbe.org/6xgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xgt RCSB], [https://www.ebi.ac.uk/pdbsum/6xgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xgt ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Cyanase catalyzes the bicarbonate-dependent degradation of cyanate to produce ammonia and carbon dioxide, and ammonia is a considerable alternative nitrogen source. Strikingly, the cyanase from the thermophilic fungus Thermomyces lanuginosus (Tl-Cyn) has the highest catalytic efficiency reported among these enzymes. However, its molecular mechanism of action is not clearly understood, because currently there is no structural information available on fungal cyanases. Here we report the crystal structure of Tl-Cyn in complex with inhibitors malonate and formate at 2.2 A resolution. The structure reveals extensive interactions at the subunit interfaces in a dimer, and a decamer is formed by a pentamer of these dimers. Our biochemical, kinetic and mutagenesis studies confirm the structural observations on the complex and provide further insights into its catalytic mechanism and inhibition. The structure has also aided the creation of a mutant enzyme with enhanced catalytic activity, and such enzymes may have the potential for biotechnological applications, including biotransformation and bioremediation. Moreover, other fungal cyanases with potentially high catalytic activity could also be predicted based on the Tl-Cyn structure, as the active site region among fungal cyanases are highly conserved.

Crystal structure of a thermophilic fungal cyanase and its implications on the catalytic mechanism for bioremediation.,Ranjan B, Choi PH, Pillai S, Permaul K, Tong L, Singh S Sci Rep. 2021 Jan 11;11(1):277. doi: 10.1038/s41598-020-79489-3. PMID:33431973<ref>PMID:33431973</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermomyces lanuginosus]]
[[Category: Choi PH]]
[[Category: Ranjan B]]
[[Category: Tong L]]