7eqm: Difference between revisions
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==Apo Truncated VhChiP (Delta 1-19)== | |||
<StructureSection load='7eqm' size='340' side='right'caption='[[7eqm]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7eqm]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_harveyi Vibrio harveyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EQM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EQM 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]] 2.5000238Å</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=7eqm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7eqm OCA], [https://pdbe.org/7eqm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7eqm RCSB], [https://www.ebi.ac.uk/pdbsum/7eqm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7eqm ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/L0RVU0_VIBHA L0RVU0_VIBHA] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
VhChiP is a chitooligosaccharide-specific porin identified in the outer membrane of Vibrio campbellii type strain American Type Culture Collection BAA 1116. VhChiP contains three identical subunits, and in each subunit, the 19-amino acid N-terminal segment serves as a molecular plug (the "N-plug") that controls the closed/open dynamics of the neighboring pores. In this study, the crystal structures of VhChiP lacking the N-plug were determined in the absence and presence of chitohexaose. Binding studies of sugar-ligand interactions by single-channel recordings and isothermal microcalorimetry experiments suggested that the deletion of the N-plug peptide significantly weakened the sugar-binding affinity due to the loss of hydrogen bonds around the central affinity sites. Steered molecular dynamic simulations revealed that the movement of the sugar chain along the sugar passage triggered the ejection of the N-plug, while the H-bonds transiently formed between the reducing end GlcNAc units of the sugar chain with the N-plug peptide may help to facilitate sugar translocation. The findings enable us to propose the structural displacement model, which enables us to understand the molecular basis of chitooligosaccharide uptake by marine Vibrio bacteria. | |||
Structural displacement model of chitooligosaccharide transport through chitoporin.,Sanram S, Aunkham A, Robinson R, Suginta W J Biol Chem. 2023 Aug;299(8):105000. doi: 10.1016/j.jbc.2023.105000. Epub 2023 , Jul 1. PMID:37394001<ref>PMID:37394001</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7eqm" style="background-color:#fffaf0;"></div> | ||
[[Category: Aunkham | |||
[[Category: Sanram | ==See Also== | ||
*[[Porin 3D structures|Porin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Vibrio harveyi]] | |||
[[Category: Aunkham A]] | |||
[[Category: Sanram S]] | |||
[[Category: Suginta W]] | |||
Latest revision as of 16:12, 21 August 2024
Apo Truncated VhChiP (Delta 1-19)Apo Truncated VhChiP (Delta 1-19)
Structural highlights
FunctionPublication Abstract from PubMedVhChiP is a chitooligosaccharide-specific porin identified in the outer membrane of Vibrio campbellii type strain American Type Culture Collection BAA 1116. VhChiP contains three identical subunits, and in each subunit, the 19-amino acid N-terminal segment serves as a molecular plug (the "N-plug") that controls the closed/open dynamics of the neighboring pores. In this study, the crystal structures of VhChiP lacking the N-plug were determined in the absence and presence of chitohexaose. Binding studies of sugar-ligand interactions by single-channel recordings and isothermal microcalorimetry experiments suggested that the deletion of the N-plug peptide significantly weakened the sugar-binding affinity due to the loss of hydrogen bonds around the central affinity sites. Steered molecular dynamic simulations revealed that the movement of the sugar chain along the sugar passage triggered the ejection of the N-plug, while the H-bonds transiently formed between the reducing end GlcNAc units of the sugar chain with the N-plug peptide may help to facilitate sugar translocation. The findings enable us to propose the structural displacement model, which enables us to understand the molecular basis of chitooligosaccharide uptake by marine Vibrio bacteria. Structural displacement model of chitooligosaccharide transport through chitoporin.,Sanram S, Aunkham A, Robinson R, Suginta W J Biol Chem. 2023 Aug;299(8):105000. doi: 10.1016/j.jbc.2023.105000. Epub 2023 , Jul 1. PMID:37394001[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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