View source for 22hl


==Beta-1,2-glucan-binding protein soaked with cyclic beta-1,2-glucoeicosaose==
<StructureSection load='22hl' size='340' side='right'caption='[[22hl]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[22hl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chloroflexus_aurantiacus_Y-400-fl Chloroflexus aurantiacus Y-400-fl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=22HL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=22HL 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]] 1.37&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=22hl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=22hl OCA], [https://pdbe.org/22hl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=22hl RCSB], [https://www.ebi.ac.uk/pdbsum/22hl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=22hl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A9WCS2_CHLAA A9WCS2_CHLAA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-1,2-Glucans are glucose polymers widely distributed in nature and play various physiological roles in the interactions between organisms such as pathogenicity and symbiosis. While various beta-1,2-glucan-degrading enzymes have been identified recently, transporters incorporating beta-1,2-glucans are still poorly characterized. In this study, we have found a beta-1,2-glucan binding protein of ABC transporter from Chloroflexus aurantiacus Y-400-fl, a filamentous anoxygenic phototrophic bacterium. The protein showed a clear affinity for linear beta-1,2-glucan in the gel shift assay. Isothermal titration calorimetric analysis revealed high binding affinities for both linear and cyclic beta-1,2-glucans, unlike for the barley beta-glucan. The recorded binding constants were high for the binding of the ABC transporter to beta-1,2-glucans. The observed unfavorable negative entropy change may have resulted from conformational restraints upon complex formation. Complex structures with linear beta-1,2-glucan and cyclic beta-1,2-glucans with degrees of polymerization of 17-20 were obtained using X-ray crystallography. Ten glucose units, designated A-J from the nonreducing end, were shared among the substrates in the complexes. Unit G is recognized by W74, W308, and D336, which are highly conserved residues within the phylogenetic group Chy400_4166. The substrate-binding mode of Chy400_4166 is completely different from that of the beta-1,2-glucooligosaccharide-binding protein from Listeria innocua. The discovery of a new type of beta-1,2-glucan-related binding protein has expanded our understanding of the metabolism of beta-1,2-glucans.

Structural and thermodynamic analyses of a novel beta-1,2-glucan binding mode in the ABC transporter solute-binding protein Chy400_4166 from Chloroflexus aurantiacus.,Kato K, Kaneko T, Hirayama R, Tanaka N, Nakai H, Torigoe H, Nakajima M FEBS J. 2026 May 10. doi: 10.1111/febs.70576. PMID:42108234<ref>PMID:42108234</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 22hl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Chloroflexus aurantiacus Y-400-fl]]
[[Category: Large Structures]]
[[Category: Hirayama R]]
[[Category: Nakajima M]]