View source for 7cbw


==Blasnase-T13A with D-asn==
<StructureSection load='7cbw' size='340' side='right'caption='[[7cbw]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cbw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_paralicheniformis Bacillus paralicheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CBW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CBW 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]] 1.978&#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=MG:MAGNESIUM+ION'>MG</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=7cbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cbw OCA], [https://pdbe.org/7cbw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cbw RCSB], [https://www.ebi.ac.uk/pdbsum/7cbw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cbw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A6I7U6Y2_9BACI A0A6I7U6Y2_9BACI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
l-Asparaginase, which catalyzes the hydrolysis of l-asparagine, is an important enzyme in both the clinical and food industry. Exploration of efficient l-asparaginase with high substrate specificity, especially high chiral selectivity, is essential for extending its use. Herein, various crystal structures of type I l-asparaginase from Bacillus licheniformis (BlAsnase) have been resolved, and we found that there are two additional tyrosines in BlAsnase, contributing to the binding and catalysis of d-asparagine. Strikingly, the substitution of Tyr278 with methionine impaired the interaction with d-asparagine via water molecules due to the small hydrophobic side chain of methionine, which forced the ligand to the deep side of the active site toward the catalytic residues and thus resulted in the loss of hydrolyzing function. Our investigation of the substrate recognition mechanism of BlAsnase is significant for both a better understanding of l-asparaginase and its rational design to achieve high specificity for clinical and industrial applications.

Structures of l-asparaginase from Bacillus licheniformis Reveal an Essential Residue for its Substrate Stereoselectivity.,Ran T, Jiao L, Wang W, Chen J, Chi H, Lu Z, Zhang C, Xu D, Lu F J Agric Food Chem. 2021 Jan 13;69(1):223-231. doi: 10.1021/acs.jafc.0c06609. Epub, 2020 Dec 28. PMID:33371681<ref>PMID:33371681</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cbw" style="background-color:#fffaf0;"></div>

==See Also==
*[[Asparaginase 3D structures|Asparaginase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus paralicheniformis]]
[[Category: Large Structures]]
[[Category: Jiao L]]
[[Category: Lu F]]
[[Category: Ran T]]
[[Category: Wang W]]