View source for 8x2w


==Crystal structure of the ancestral GH19 chitinase, Anc4+LoopII (P12K/N13H/S58T/N193G/Y194F/D197R)==
<StructureSection load='8x2w' size='340' side='right'caption='[[8x2w]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8x2w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8X2W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8X2W 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]] 1.4&#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=8x2w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8x2w OCA], [https://pdbe.org/8x2w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8x2w RCSB], [https://www.ebi.ac.uk/pdbsum/8x2w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8x2w ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Loops are small secondary structural elements that play a crucial role in the emergence of new enzyme functions. However, the evolutionary molecular mechanisms how proteins acquire these loop elements and obtain new function is poorly understood. To address this question, we study glycoside hydrolase family 19 (GH19) chitinase-an essential enzyme family for pathogen degradation in plants. By revealing the evolutionary history and loops appearance of GH19 chitinase, we discover that one loop which is remote from the catalytic site, is necessary to acquire the new antifungal activity. We demonstrate that this remote loop directly accesses the fungal cell wall, and surprisingly, it needs to adopt a defined structure supported by long-range intramolecular interactions to perform its function. Our findings prove that nature applies this strategy at the molecular level to achieve a complex biological function while maintaining the original activity in the catalytic pocket, suggesting an alternative way to design new enzyme function.

Remote loop evolution reveals a complex biological function for chitinase enzymes beyond the active site.,Kozome D, Sljoka A, Laurino P Nat Commun. 2024 Apr 15;15(1):3227. doi: 10.1038/s41467-024-47588-8. PMID:38622119<ref>PMID:38622119</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 8x2w" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Kozome D]]
[[Category: Laurino P]]