7cbr: Difference between revisions
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==Blasnase-T13A with D-asn== | ==Blasnase-T13A with D-asn== | ||
<StructureSection load='7cbr' size='340' side='right'caption='[[7cbr]]' scene=''> | <StructureSection load='7cbr' size='340' side='right'caption='[[7cbr]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CBR FirstGlance]. <br> | <table><tr><td colspan='2'>[[7cbr]] 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=7CBR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CBR FirstGlance]. <br> | ||
</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=7cbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cbr OCA], [https://pdbe.org/7cbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cbr RCSB], [https://www.ebi.ac.uk/pdbsum/7cbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cbr ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DSG:D-ASPARAGINE'>DSG</scene>, <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=7cbr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cbr OCA], [https://pdbe.org/7cbr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cbr RCSB], [https://www.ebi.ac.uk/pdbsum/7cbr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cbr ProSAT]</span></td></tr> | |||
</table> | </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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7cbr" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Asparaginase 3D structures|Asparaginase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus paralicheniformis]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Jiao L]] | [[Category: Jiao L]] | ||
Latest revision as of 19:02, 29 November 2023
Blasnase-T13A with D-asnBlasnase-T13A with D-asn
Structural highlights
FunctionPublication Abstract from PubMedl-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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