View source for 5yzk


==Solution structure of LysM domain from a chitinase derived from Volvox carteri==
<StructureSection load='5yzk' size='340' side='right'caption='[[5yzk]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5yzk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Volvox_carteri_f._nagariensis Volvox carteri f. nagariensis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YZK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YZK 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=5yzk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yzk OCA], [https://pdbe.org/5yzk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yzk RCSB], [https://www.ebi.ac.uk/pdbsum/5yzk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yzk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D8UFB5_VOLCA D8UFB5_VOLCA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Two N-terminal lysin motifs (LysMs) found in a chitinase from the green alga Volvox carteri (VcLysM1 and VcLysM2) were produced, and their structures and chitin-binding properties were characterized. The binding affinities of VcLysM1 toward chitin oligomers determined by isothermal titration calorimetry (ITC) were higher than those of VcLysM2 by 0.8-1.1 kcal/mol of DeltaG degrees . Based on the NMR solution structures of the two LysMs, the differences in binding affinities were found to result from amino acid substitutions at the binding site. The NMR spectrum of a two-domain protein (VcLysM1+2), in which VcLysM1 and VcLysM2 are linked in tandem through a flexible linker, suggested that the individual domains of VcLysM1+2 independently fold and do not interact with each other. ITC analysis of chitin-oligomer binding revealed two different binding sites in VcLysM1+2, showing no cooperativity. The binding affinities of the VcLysM1 domain in VcLysM1+2 were lower than those of VcLysM1 alone, probably due to the flexible linker destabilizing the interaction between the chito-oligosaccahrides and VcLysM1 domain. Overall, two LysMs attached to the chitinase from the primitive plant species, V. carteri, were found to resemble bacterial LysMs reported thus far.

Structures and chitin-binding properties of two N-terminal lysin motifs (LysMs) found in a chitinase from Volvox carteri.,Kitaoku Y, Nishimura S, Hirono T, Suginta W, Ohnuma T, Fukamizo T Glycobiology. 2019 Jul 1;29(7):565-575. doi: 10.1093/glycob/cwz024. PMID:30976779<ref>PMID:30976779</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5yzk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Volvox carteri f. nagariensis]]
[[Category: Fukamizo T]]
[[Category: Kitaoku Y]]
[[Category: Nishimura S]]
[[Category: Ohnuma T]]