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4k6h

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Revision as of 11:33, 4 August 2016

Crystal structure of CALB mutant L278M from Candida antarctica

Structural highlights

4k6h is a 2 chain structure with sequence from Canar. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4k5q, 4k6g, 4k6k
Activity:	Triacylglycerol lipase, with EC number 3.1.1.3
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LIPB_CANAR] Hydrolysis of triglycerides. Is very stereospecific both in hydrolysis and in organic synthesis and has a potentially important application in glucolipid synthesis.

Publication Abstract from PubMed

Enzyme stability is an important issue for protein engineers. Understanding how rigidity in the active site affects protein kinetic stability will provide new insight into enzyme stabilization. In this study, we demonstrated enhanced kinetic stability of Candida antarctica lipase B (CalB) by mutating the structurally flexible residues within the active site. Six residues within 10 A of the catalytic Ser(105) residue with a high B factor were selected for iterative saturation mutagenesis. After screening 2200 colonies, we obtained the D223G/L278M mutant, which exhibited a 13-fold increase in half-life at 48 degrees C and a 12 degrees C higher T50(15), the temperature at which enzyme activity is reduced to 50% after a 15-min heat treatment. Further characterization showed that global unfolding resistance against both thermal and chemical denaturation also improved. Analysis of the crystal structures of wild-type CalB and the D223G/L278M mutant revealed that the latter formed an extra main chain hydrogen bond network with seven structurally coupled residues within the flexible alpha10 helix that are primarily involved in forming the active site. Further investigation of the relative B factor profile and molecular dynamics simulation confirmed that the enhanced rigidity decreased fluctuation of the active site residues at high temperature. These results indicate that enhancing the rigidity of the flexible segment within the active site may provide an efficient method for improving enzyme kinetic stability.

Enhanced enzyme kinetic stability by increasing rigidity within the active site.,Xie Y, An J, Yang G, Wu G, Zhang Y, Cui L, Feng Y J Biol Chem. 2014 Mar 14;289(11):7994-8006. doi: 10.1074/jbc.M113.536045. Epub, 2014 Jan 21. PMID:24448805^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Xie Y, An J, Yang G, Wu G, Zhang Y, Cui L, Feng Y. Enhanced enzyme kinetic stability by increasing rigidity within the active site. J Biol Chem. 2014 Mar 14;289(11):7994-8006. doi: 10.1074/jbc.M113.536045. Epub, 2014 Jan 21. PMID:24448805 doi:http://dx.doi.org/10.1074/jbc.M113.536045

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4k6h"

@@ Line 1: / Line 1: @@
 ==Crystal structure of CALB mutant L278M from Candida antarctica==
 <StructureSection load='4k6h' size='340' side='right' caption='[[4k6h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4k5q|4k5q]], [[4k6g|4k6g]], [[4k6k|4k6k]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k6h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k6h RCSB], [http://www.ebi.ac.uk/pdbsum/4k6h PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k6h OCA], [http://pdbe.org/4k6h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k6h RCSB], [http://www.ebi.ac.uk/pdbsum/4k6h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k6h ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4k6h" style="background-color:#fffaf0;"></div>
 ==See Also==

4k6h

From Proteopedia

Revision as of 11:33, 4 August 2016

Crystal structure of CALB mutant L278M from Candida antarctica

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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