4a2m

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Current revision (07:13, 1 May 2024) (edit) (undo)
 
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<StructureSection load='4a2m' size='340' side='right'caption='[[4a2m]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<StructureSection load='4a2m' size='340' side='right'caption='[[4a2m]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4a2m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bactn Bactn]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A2M FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4a2m]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron_VPI-5482 Bacteroides thetaiotaomicron VPI-5482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A2M FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCD:4,5-DEHYDRO-D-GLUCURONIC+ACID'>GCD</scene>, <scene name='pdbligand=NGS:2-(ACETYLAMINO)-2-DEOXY-6-O-SULFO-BETA-D-GLUCOPYRANOSE'>NGS</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4a2l|4a2l]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GCD:4,5-DEHYDRO-D-GLUCURONIC+ACID'>GCD</scene>, <scene name='pdbligand=NGS:2-(ACETYLAMINO)-2-DEOXY-6-O-SULFO-BETA-D-GLUCOPYRANOSE'>NGS</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=4a2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2m OCA], [https://pdbe.org/4a2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a2m RCSB], [https://www.ebi.ac.uk/pdbsum/4a2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a2m ProSAT]</span></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=4a2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2m OCA], [https://pdbe.org/4a2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a2m RCSB], [https://www.ebi.ac.uk/pdbsum/4a2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a2m ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q89YR8_BACTN Q89YR8_BACTN]
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Signaling across the membrane in response to extracellular stimuli is essential for survival of all cells. In bacteria, responses to environmental changes are predominantly mediated by two-component systems, which are typically composed of a membrane-spanning sensor histidine kinase and a cytoplasmic response regulator. In the human gut symbiont Bacteroides thetaiotaomicron, hybrid two-component systems are a key part of the bacterium's ability to sense and degrade complex carbohydrates in the gut. Here, we identify the activating ligand of the hybrid two-component system, BT4663, which controls heparin and heparan sulfate acquisition and degradation in this prominent gut microbe, and report the crystal structure of the extracellular sensor domain in both apo and ligand-bound forms. Current models for signal transduction across the membrane involve either a piston-like or rotational displacement of the transmembrane helices to modulate activity of the linked cytoplasmic kinases. The structures of the BT4663 sensor domain reveal a significant conformational change in the homodimer on ligand binding, which results in a scissor-like closing of the C-termini of each protomer. We propose this movement activates the attached intracellular kinase domains and represents an allosteric mechanism for bacterial transmembrane signaling distinct from previously described models, thus expanding our understanding of signal transduction across the membrane, a fundamental requirement in many important biological processes.
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A scissor blade-like closing mechanism implicated in transmembrane signaling in a Bacteroides hybrid two-component system.,Lowe EC, Basle A, Czjzek M, Firbank SJ, Bolam DN Proc Natl Acad Sci U S A. 2012 May 8;109(19):7298-303. Epub 2012 Apr 24. PMID:22532667<ref>PMID:22532667</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4a2m" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bactn]]
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[[Category: Bacteroides thetaiotaomicron VPI-5482]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Basle, A]]
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[[Category: Basle A]]
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[[Category: Bolam, D N]]
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[[Category: Bolam DN]]
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[[Category: Czjzek, M]]
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[[Category: Czjzek M]]
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[[Category: Firbank, S J]]
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[[Category: Firbank SJ]]
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[[Category: Lowe, E C]]
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[[Category: Lowe EC]]
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[[Category: Beta-propeller]]
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[[Category: Transcription]]
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Current revision

Structure of the periplasmic domain of the heparin and heparan sulphate sensing hybrid two component system BT4663 in apo and ligand bound forms

PDB ID 4a2m

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