3ox0: Difference between revisions
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<StructureSection load='3ox0' size='340' side='right'caption='[[3ox0]], [[Resolution|resolution]] 3.05Å' scene=''> | <StructureSection load='3ox0' size='340' side='right'caption='[[3ox0]], [[Resolution|resolution]] 3.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ox0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OX0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[3ox0]] is a 2 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=3OX0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OX0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.049Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CCC:CYTIDINE-5-PHOSPHATE-2,3-CYCLIC+PHOSPHATE'>CCC</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3ox0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ox0 OCA], [https://pdbe.org/3ox0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ox0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ox0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ox0 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=3ox0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ox0 OCA], [https://pdbe.org/3ox0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ox0 RCSB], [https://www.ebi.ac.uk/pdbsum/3ox0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ox0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Vibrio cholerae]] | ||
[[Category: | [[Category: Huang L]] | ||
[[Category: | [[Category: Patel DJ]] | ||
[[Category: | [[Category: Serganov A]] | ||
Latest revision as of 12:45, 6 September 2023
Crystal structure of glycine riboswitch, unbound stateCrystal structure of glycine riboswitch, unbound state
Structural highlights
Publication Abstract from PubMedGlycine riboswitches regulate gene expression by feedback modulation in response to cooperative binding to glycine. Here, we report on crystal structures of the second glycine-sensing domain from the Vibrio cholerae riboswitch in the ligand-bound and unbound states. This domain adopts a three-helical fold that centers on a three-way junction and accommodates glycine within a bulge-containing binding pocket above the junction. Glycine recognition is facilitated by a pair of bound Mg(2+) cations and governed by specific interactions and shape complementarity with the pocket. A conserved adenine extrudes from the binding pocket and intercalates into the junction implying that glycine binding in the context of the complete riboswitch could impact on gene expression by stabilizing the riboswitch junction and regulatory P1 helix. Analysis of riboswitch interactions in the crystal and footprinting experiments indicates that adjacent glycine-sensing modules of the riboswitch could form specific interdomain interactions, thereby potentially contributing to the cooperative response. Structural insights into ligand recognition by a sensing domain of the cooperative glycine riboswitch.,Huang L, Serganov A, Patel DJ Mol Cell. 2010 Dec 10;40(5):774-86. PMID:21145485[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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