4h4l: Difference between revisions
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==Crystal Structure of ternary complex of HutP(HutP-L-His-Zn)== | ==Crystal Structure of ternary complex of HutP(HutP-L-His-Zn)== | ||
<StructureSection load='4h4l' size='340' side='right' caption='[[4h4l]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4h4l' size='340' side='right'caption='[[4h4l]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4h4l]] is a 12 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4h4l]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2zh0 2zh0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H4L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H4L FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HIS:HISTIDINE'>HIS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4h4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h4l OCA], [https://pdbe.org/4h4l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h4l RCSB], [https://www.ebi.ac.uk/pdbsum/4h4l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h4l ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/HUTP_BACSU HUTP_BACSU] Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization.[HAMAP-Rule:MF_00779] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4h4l" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
[[Category: Large Structures]] | |||
[[Category: Dhakshnamoorthy B]] | |||
[[Category: | [[Category: Kumar PKR]] | ||
[[Category: | [[Category: Misono TS]] | ||
[[Category: | [[Category: Mizuno H]] | ||
[[Category: | |||
[[Category: | |||
Latest revision as of 17:04, 8 November 2023
Crystal Structure of ternary complex of HutP(HutP-L-His-Zn)Crystal Structure of ternary complex of HutP(HutP-L-His-Zn)
Structural highlights
FunctionHUTP_BACSU Antiterminator that binds to cis-acting regulatory sequences on the mRNA in the presence of histidine, thereby suppressing transcription termination and activating the hut operon for histidine utilization.[HAMAP-Rule:MF_00779] Publication Abstract from PubMedAnti-terminator proteins control gene expression by recognizing control signals within cognate transcripts and then preventing transcription termination. HutP is such a regulatory protein that regulates the expression of the histidine utilization (hut) operon in Bacillus subtilis by binding to cis-acting regulatory sequences in hut mRNAs. During the anti-termination process, l-histidine and a divalent ion are required for hutP to bind to the specific sequence within the hut mRNA. Our previous crystal structure of the HutP-l-histidine-Mg2+-RNA ternary complex demonstrated that the l-histidine ligand and Mg2+ bind together such that the backbone nitrogen and carboxyl oxygen of l-histidine coordinate with Mg2+. In addition to the Mg2+, other divalent ions are also known to efficiently support the l-histidine-dependent anti-termination of the hut operon, and the best divalent ion is Zn2+. In this study, we determined the crystal structure of the HutP-l-histidine-Zn2+ complex and found that the orientation of l-histidine coordinated to Zn2+ is reversed relative to that of l-histidine coordinated to Mg2+, i.e., the imidazole side chain nitrogen of l-histidine coordinates to Zn2+. This alternative binding mode of the l-histidine ligand to a divalent ion provides further insight into the mechanisms responsible for the activation of RNA binding during the hut anti-termination process. Alternative binding modes of l-histidine guided by metal ions for the activation of the antiterminator protein HutP of Bacillus subtilis.,Dhakshnamoorthy B, Mizuno H, Kumar PK J Struct Biol. 2013 Jun 5. pii: S1047-8477(13)00151-2. doi:, 10.1016/j.jsb.2013.05.019. PMID:23748184[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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