4lvz: Difference between revisions

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==Structure of the THF riboswitch bound to 2,6-diaminopurine==
==Structure of the THF riboswitch bound to 2,6-diaminopurine==
<StructureSection load='4lvz' size='340' side='right' caption='[[4lvz]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
<StructureSection load='4lvz' size='340' side='right'caption='[[4lvz]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4lvz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LVZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4lvz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LVZ FirstGlance]. <br>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Batey, R T]]
[[Category: Batey, R T]]
[[Category: Trausch, J J]]
[[Category: Trausch, J J]]

Revision as of 12:02, 3 April 2019

Structure of the THF riboswitch bound to 2,6-diaminopurineStructure of the THF riboswitch bound to 2,6-diaminopurine

Structural highlights

4lvz 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

The tetrahydrofolate (THF) riboswitch regulates folate transport and metabolism in a number of Firmicutes by cooperatively binding two molecules of THF. To further understand this riboswitch's specificity for THF, binding and regulatory activity of a series of THF analogs and antifolates were examined. Our data reveal that although binding is dominated by the RNA's interactions with the pterin moiety, the para-aminobenzoic acid (pABA) moiety plays a significant role in transcriptional regulation. Further, we find that adenine and several other analogs bind with high affinity by an alternative binding mechanism. Despite a similar affinity to THF, adenine is a poor regulator of transcriptional attenuation. These results demonstrate that binding alone does not determine a compound's effectiveness in regulating the activity of the riboswitch-a complication in current efforts to develop antimicrobials that target these RNAs.

A Disconnect between High-Affinity Binding and Efficient Regulation by Antifolates and Purines in the Tetrahydrofolate Riboswitch.,Trausch JJ, Batey RT Chem Biol. 2014 Feb 20;21(2):205-16. doi: 10.1016/j.chembiol.2013.11.012. Epub, 2014 Jan 2. PMID:24388757[1]

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

See Also

References

  1. Trausch JJ, Batey RT. A Disconnect between High-Affinity Binding and Efficient Regulation by Antifolates and Purines in the Tetrahydrofolate Riboswitch. Chem Biol. 2014 Feb 20;21(2):205-16. doi: 10.1016/j.chembiol.2013.11.012. Epub, 2014 Jan 2. PMID:24388757 doi:http://dx.doi.org/10.1016/j.chembiol.2013.11.012

4lvz, resolution 1.77Å

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