View source for 7buk


==T1 lipase mutant - 5M (D43E/T118N/E226D/E250L/N304E)==
<StructureSection load='7buk' size='340' side='right'caption='[[7buk]], [[Resolution|resolution]] 2.64&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7buk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_zalihae Geobacillus zalihae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BUK 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]] 2.644&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <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=7buk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7buk OCA], [https://pdbe.org/7buk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7buk RCSB], [https://www.ebi.ac.uk/pdbsum/7buk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7buk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q842J9_9BACI Q842J9_9BACI] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
5M mutant lipase was derived through cumulative mutagenesis of amino acid residues (D43E/T118N/E226D/E250L/N304E) of T1 lipase from Geobacillus zalihae. A previous study revealed that cumulative mutations in 5M mutant lipase resulted in decreased thermostability compared to wild-type T1 lipase. Multiple amino acids substitution might cause structural destabilization due to negative cooperation. Hence, the three-dimensional structure of 5M mutant lipase was elucidated to determine the evolution in structural elements caused by amino acids substitution. A suitable crystal for X-ray diffraction was obtained from an optimized formulation containing 0.5 M sodium cacodylate trihydrate, 0.4 M sodium citrate tribasic pH 6.4 and 0.2 M sodium chloride with 2.5 mg/mL protein concentration. The three-dimensional structure of 5M mutant lipase was solved at 2.64 A with two molecules per asymmetric unit. The detailed analysis of the structure revealed that there was a decrease in the number of molecular interactions, including hydrogen bonds and ion interactions, which are important in maintaining the stability of lipase. This study facilitates understanding of and highlights the importance of hydrogen bonds and ion interactions towards protein stability. Substrate specificity and docking analysis on the open structure of 5M mutant lipase revealed changes in substrate preference. The molecular dynamics simulation of 5M-substrates complexes validated the substrate preference of 5M lipase towards long-chain p-nitrophenyl-esters.

Structure elucidation and docking analysis of 5M mutant of T1 lipase Geobacillus zalihae.,Ishak SNH, Kamarudin NHA, Ali MSM, Leow ATC, Shariff FM, Rahman RNZRA PLoS One. 2021 Jun 1;16(6):e0251751. doi: 10.1371/journal.pone.0251751., eCollection 2021. PMID:34061877<ref>PMID:34061877</ref>

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

==See Also==
*[[Lipase 3D Structures|Lipase 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Geobacillus zalihae]]
[[Category: Large Structures]]
[[Category: Ali MSM]]
[[Category: Ishak SNH]]
[[Category: Kamarudin NHA]]
[[Category: Leow ATC]]
[[Category: Rahman RNZRA]]