8ylh: Difference between revisions
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==Crystal structure of Pectobacterium atrosepticum PecS== | |||
<StructureSection load='8ylh' size='340' side='right'caption='[[8ylh]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8ylh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_atrosepticum Pectobacterium atrosepticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8YLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8YLH 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]] 1.55Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=8ylh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ylh OCA], [https://pdbe.org/8ylh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ylh RCSB], [https://www.ebi.ac.uk/pdbsum/8ylh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ylh ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q6D5K4_PECAS Q6D5K4_PECAS] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Uric acid (UA)-responsive transcriptional regulators (UrtRs), which belong to the multiple antibiotic resistance regulator (MarR) superfamily, transcriptionally coordinate virulence and metabolism in bacteria by modulating interactions with operator DNA in response to UA. To elucidate the transcriptional regulatory mechanism of UrtR, we structurally analyzed UrtR proteins, including PecS, MftR, and HucR, alone and in complex with UA or DNA. UrtR contains a dimerization domain (DD) and a winged helix-turn-helix domain (wHTHD) and forms a homodimer primarily via the DD, as observed for other MarR superfamily proteins. However, UrtRs are characterized by a unique N-terminal alpha-helix, which contributes to dimerization and UA recognition. In the absence of UA, the UrtR dimer symmetrically binds to the operator double-stranded DNA (dsDNA) by inserting its alpha4 recognition helix and beta-stranded wing within the wHTHD into the major and minor grooves of dsDNA, respectively. Upon exposure to UA, UrtR accommodates UA in the intersubunit pocket between the DD and wHTHD. UA binding induces a conformational change in the major groove-binding core element of the UrtR wHTHD, generating a DNA binding-incompatible structure. This local allosteric mechanism of UrtR completely differs from that generally observed in other MarR superfamily members, in which the entire wHTHD undergoes effector-responsive global shifts. | |||
Structural basis of transcriptional regulation by UrtR in response to uric acid.,Song WS, Ki DU, Cho HY, Kwon OH, Cho H, Yoon SI Nucleic Acids Res. 2024 Nov 27;52(21):13192-13205. doi: 10.1093/nar/gkae922. PMID:39484741<ref>PMID:39484741</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8ylh" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pectobacterium atrosepticum]] | |||
[[Category: Song WS]] | |||
[[Category: Yoon SI]] | |||
Latest revision as of 09:29, 4 December 2024
Crystal structure of Pectobacterium atrosepticum PecSCrystal structure of Pectobacterium atrosepticum PecS
Structural highlights
FunctionPublication Abstract from PubMedUric acid (UA)-responsive transcriptional regulators (UrtRs), which belong to the multiple antibiotic resistance regulator (MarR) superfamily, transcriptionally coordinate virulence and metabolism in bacteria by modulating interactions with operator DNA in response to UA. To elucidate the transcriptional regulatory mechanism of UrtR, we structurally analyzed UrtR proteins, including PecS, MftR, and HucR, alone and in complex with UA or DNA. UrtR contains a dimerization domain (DD) and a winged helix-turn-helix domain (wHTHD) and forms a homodimer primarily via the DD, as observed for other MarR superfamily proteins. However, UrtRs are characterized by a unique N-terminal alpha-helix, which contributes to dimerization and UA recognition. In the absence of UA, the UrtR dimer symmetrically binds to the operator double-stranded DNA (dsDNA) by inserting its alpha4 recognition helix and beta-stranded wing within the wHTHD into the major and minor grooves of dsDNA, respectively. Upon exposure to UA, UrtR accommodates UA in the intersubunit pocket between the DD and wHTHD. UA binding induces a conformational change in the major groove-binding core element of the UrtR wHTHD, generating a DNA binding-incompatible structure. This local allosteric mechanism of UrtR completely differs from that generally observed in other MarR superfamily members, in which the entire wHTHD undergoes effector-responsive global shifts. Structural basis of transcriptional regulation by UrtR in response to uric acid.,Song WS, Ki DU, Cho HY, Kwon OH, Cho H, Yoon SI Nucleic Acids Res. 2024 Nov 27;52(21):13192-13205. doi: 10.1093/nar/gkae922. PMID:39484741[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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