2hol: Difference between revisions

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<StructureSection load='2hol' size='340' side='right'caption='[[2hol]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='2hol' size='340' side='right'caption='[[2hol]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2hol]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HOL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HOL FirstGlance]. <br>
<table><tr><td colspan='2'>[[2hol]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HOL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HOL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hoj|2hoj]], [[2hok|2hok]], [[2hom|2hom]], [[2hoo|2hoo]], [[2hop|2hop]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hoj|2hoj]], [[2hok|2hok]], [[2hom|2hom]], [[2hoo|2hoo]], [[2hop|2hop]]</div></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hol OCA], [http://pdbe.org/2hol PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hol RCSB], [http://www.ebi.ac.uk/pdbsum/2hol PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hol 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=2hol FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hol OCA], [https://pdbe.org/2hol PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hol RCSB], [https://www.ebi.ac.uk/pdbsum/2hol PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hol ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">

Revision as of 14:11, 5 January 2022

Crystal structure of an E. coli thi-box riboswitch bound to thiamine pyrophosphate, barium ionsCrystal structure of an E. coli thi-box riboswitch bound to thiamine pyrophosphate, barium ions

Structural highlights

2hol is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Riboswitches are noncoding mRNA elements that bind small-molecule metabolites with high affinity and specificity, and they regulate the expression of associated genes. The thi-box riboswitch can exhibit a 1000-fold higher affinity for thiamine pyrophosphate over closely related noncognate compounds such as thiamine monophosphate. To understand the chemical basis of thi-box pyrophosphate specificity, we have determined crystal structures of an E. coli thi-box bound to thiamine pyrophosphate, thiamine monophosphate, and the structural analogs benfotiamine and pyrithiamine. When bound to monophosphorylated compounds, the RNA elements that recognize the thiamine and phosphate moieties of the ligand move closer together. This allows the riboswitch to recognize the monophosphate in a manner similar to how it recognizes the beta-phosphate of thiamine pyrophosphate. In the pyrithiamine complex, the pyrophosphate binding site is largely unstructured. These results show how the riboswitch can bind to various metabolites, and why the thi-box preferentially binds thiamine pyrophosphate.

Crystal structures of the thi-box riboswitch bound to thiamine pyrophosphate analogs reveal adaptive RNA-small molecule recognition.,Edwards TE, Ferre-D'Amare AR Structure. 2006 Sep;14(9):1459-68. PMID:16962976[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Edwards TE, Ferre-D'Amare AR. Crystal structures of the thi-box riboswitch bound to thiamine pyrophosphate analogs reveal adaptive RNA-small molecule recognition. Structure. 2006 Sep;14(9):1459-68. PMID:16962976 doi:S0969-2126(06)00330-3

2hol, resolution 2.90Å

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