4zoq
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zoq]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZOQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[4zoq]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZOQ 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=4zoq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zoq OCA], [https://pdbe.org/4zoq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zoq RCSB], [https://www.ebi.ac.uk/pdbsum/4zoq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zoq 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]] 2.35Å</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=4zoq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zoq OCA], [https://pdbe.org/4zoq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zoq RCSB], [https://www.ebi.ac.uk/pdbsum/4zoq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zoq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q65DC7_BACLD Q65DC7_BACLD] | [https://www.uniprot.org/uniprot/Q65DC7_BACLD Q65DC7_BACLD] | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The final step of lanthipeptide biosynthesis involves the removal of leader peptides by dedicated proteases. In vitro characterization of LicP, a class II LanP protease involved in the biosynthesis of the lantibiotic lichenicidin, revealed a self-cleavage step that removes 100 amino acids from the N-terminus. The 2.35 A resolution crystal structure provides insights into the active site geometry and substrate specificity, and unveiled an unusual calcium-independent maturation mechanism of a subtilisin family member. LicP processes LicA2 peptides with or without post-translational modifications, but dehydrated and cyclized LicA2 is favored. Investigation of its substrate specificity demonstrated that LicP can serve as an efficient sequence-specific traceless protease and may have great utility in basic research and biotechnology. Encouraged by these findings for LicP, we identified 13 other class II LanPs, ten of which were previously unknown, and suggest that these proteins may serve as a pool of proteases with diverse recognition sequences for general traceless tag removal applications, expanding the current toolbox of proteases. | ||
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- | Applications of the class II lanthipeptide protease LicP for sequence-specific, traceless peptide bond cleavage.,Tang W, Dong SH, Repka LM, He C, Nair SK, van der Donk WA Chem Sci. 2015 Nov 1;6(11):6270-6279. doi: 10.1039/c5sc02329g. Epub 2015 Sep 2. PMID:30090246<ref>PMID:30090246</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 4zoq" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
Crystal Structure of a Lanthipeptide Protease
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