View source for 4zxm


==Crystal structure of PGRP domain from Branchiostoma belcheri tsingtauense peptidoglycan recognition protein 3==
<StructureSection load='4zxm' size='340' side='right'caption='[[4zxm]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4zxm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Branchiostoma_belcheri_tsingtauense Branchiostoma belcheri tsingtauense]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZXM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZXM 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]] 2.8&#8491;</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=4zxm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zxm OCA], [https://pdbe.org/4zxm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zxm RCSB], [https://www.ebi.ac.uk/pdbsum/4zxm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zxm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0R4I988_BRABE A0A0R4I988_BRABE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidoglycan recognition proteins (PGRPs), which have been identified in most animals, are pattern recognition molecules that involve antimicrobial defense. Resulting from extraordinary expansion of innate immune genes, the amphioxus encodes many PGRPs of diverse functions. For instance, three isoforms of PGRP encoded by Branchiostoma belcheri tsingtauense, termed BbtPGRP1~3, are fused with a chitin binding domain (CBD) at the N-terminus. Here we report the 2.7 A crystal structure of BbtPGRP3, revealing an overall structure of an N-terminal hevein-like CBD followed by a catalytic PGRP domain. Activity assays combined with site-directed mutagenesis indicated that the individual PGRP domain exhibits amidase activity towards both DAP-type and Lys-type peptidoglycans (PGNs), the former of which is favored. The N-terminal CBD not only has the chitin-binding activity, but also enables BbtPGRP3 to gain a five-fold increase of amidase activity towards the Lys-type PGNs, leading to a significantly broadened substrate spectrum. Together, we propose that modular evolution via domain shuffling combined with gene horizontal transfer makes BbtPGRP1~3 novel PGRPs of augmented catalytic activity and broad recognition spectrum.

Activity Augmentation of Amphioxus Peptidoglycan Recognition Protein BbtPGRP3 via Fusion with a Chitin Binding Domain.,Wang WJ, Cheng W, Luo M, Yan Q, Yu HM, Li Q, Cao DD, Huang S, Xu A, Mariuzza RA, Chen Y, Zhou CZ PLoS One. 2015 Oct 19;10(10):e0140953. doi: 10.1371/journal.pone.0140953., eCollection 2015. PMID:26479246<ref>PMID:26479246</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4zxm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Branchiostoma belcheri tsingtauense]]
[[Category: Large Structures]]
[[Category: Cheng W]]
[[Category: Jiang YL]]
[[Category: Luo M]]
[[Category: Wang WJ]]
[[Category: Yu HM]]