View source for 8i5k


==Crystal structure of chitin oligosaccharide binding protein from Vibrio cholera in complex with chitotriose.==
<StructureSection load='8i5k' size='340' side='right'caption='[[8i5k]], [[Resolution|resolution]] 1.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8i5k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I5K 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]] 1.219&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PRD_900017:triacetyl-beta-chitotriose'>PRD_900017</scene></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=8i5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i5k OCA], [https://pdbe.org/8i5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i5k RCSB], [https://www.ebi.ac.uk/pdbsum/8i5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i5k ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A085SLP2_VIBCL A0A085SLP2_VIBCL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Periplasmic solute-binding proteins (SBPs) specific for chitooligosaccharides, (GlcNAc)(n) (n = 2, 3, 4, 5 and 6), are involved in the uptake of chitinous nutrients and the negative control of chitin signal transduction in Vibrios. Most translocation processes by SBPs across the inner membrane have been explained thus far by two-domain open/closed mechanism. Here we propose three-domain mechanism of the (GlcNAc)(n) translocation based on experiments using a recombinant VcCBP, SBP specific for (GlcNAc)(n) from Vibrio cholerae. X-ray crystal structures of unliganded or (GlcNAc)(3)-liganded VcCBP solved at 1.2-1.6 A revealed three distinct domains, the Upper1, Upper2 and Lower domains for this protein. Molecular dynamics simulation indicated that the motions of the three domains are independent and that in the (GlcNAc)(3)-liganded state the Upper2/Lower interface fluctuated more intensively, compared to the Upper1/Lower interface. The Upper1/Lower interface bound two GlcNAc residues tightly, while the Upper2/Lower interface appeared to loosen and release the bound sugar molecule. The three-domain mechanism proposed here was fully supported by binding data obtained by thermal unfolding experiments and ITC, and may be applicable to other translocation systems involving SBPs belonging to the same cluster.

Periplasmic chitooligosaccharide-binding protein requires a three-domain organization for substrate translocation.,Ohnuma T, Tsujii J, Kataoka C, Yoshimoto T, Takeshita D, Lampela O, Juffer AH, Suginta W, Fukamizo T Sci Rep. 2023 Nov 23;13(1):20558. doi: 10.1038/s41598-023-47253-y. PMID:37996461<ref>PMID:37996461</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8i5k" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae]]
[[Category: Ohnuma T]]
[[Category: Takeshita D]]