View source for 6jqw


==Crystal structure of a hydrogenase from Trichosporon moniliiforme==
<StructureSection load='6jqw' size='340' side='right'caption='[[6jqw]], [[Resolution|resolution]] 1.44&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jqw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cutaneotrichosporon_moniliiforme Cutaneotrichosporon moniliiforme]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JQW 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]] 1.437&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6jqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jqw OCA], [https://pdbe.org/6jqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jqw RCSB], [https://www.ebi.ac.uk/pdbsum/6jqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jqw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SDC_CUTMO SDC_CUTMO] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Salicylic acid (SA) decarboxylase from Trichosporon moniliiforme (TmSdc), which reversibly catalyses the decarboxylation of SA to yield phenol, is of significant interest because of its potential for the production of benzoic acid derivatives under environmentally friendly reaction conditions. TmSdc showed a preference for C2 hydroxybenzoate derivatives, with kcat/Km of SA being 3.2 x 10(3) M(-1) s(-1). Here, we presented the first crystal structures of TmSdc, including a complex with SA. The three conserved residues of Glu8, His169, and Asp298 are the catalytic residues within the TIM-barrel domain of TmSdc. Trp239 forms a unique hydrophobic recognition site by interacting with the phenyl ring of SA, while Arg235 is responsible for recognizing the hydroxyl group at the C2 of SA via hydrogen bond interactions. Using a semi-rational combinatorial active-site saturation test, we obtained the TmSdc mutant MT3 (Y64T/P191G/F195V/E302D), which exhibited a 26.4-fold increase in kcat/Km with SA, reaching 8.4 x 10(4) M(-1) s(-1). Steered molecular dynamics simulations suggested that the structural changes in MT3 relieved the steric hindrance within the substrate access channel and enlarged the substrate-binding pocket, leading to the increased activity by improving substrate access. Our data elucidate the unique substrate recognition mode and the substrate entrance tunnel of SA decarboxylase.

Structural Basis of Salicylic Acid Decarboxylase Reveals a Unique Substrate Recognition Mode and Access Channel.,Gao X, Wu M, Zhang W, Li C, Guo RT, Dai Y, Liu W, Mao S, Lu F, Qin HM J Agric Food Chem. 2021 Oct 6;69(39):11616-11625. doi: 10.1021/acs.jafc.1c04091. , Epub 2021 Sep 23. PMID:34553918<ref>PMID:34553918</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jqw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Cutaneotrichosporon moniliiforme]]
[[Category: Large Structures]]
[[Category: Chen XT]]
[[Category: Qin HM]]