3mwm: Difference between revisions
No edit summary |
No edit summary |
||
Line 3: | Line 3: | ||
<StructureSection load='3mwm' size='340' side='right'caption='[[3mwm]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3mwm' size='340' side='right'caption='[[3mwm]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3mwm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3mwm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MWM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MWM 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]] 2.4Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3mwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mwm OCA], [https://pdbe.org/3mwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mwm RCSB], [https://www.ebi.ac.uk/pdbsum/3mwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mwm 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=3mwm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mwm OCA], [https://pdbe.org/3mwm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3mwm RCSB], [https://www.ebi.ac.uk/pdbsum/3mwm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3mwm ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9L2H5_STRCO Q9L2H5_STRCO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Line 22: | Line 24: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces coelicolor]] | ||
[[Category: | [[Category: An YJ]] | ||
[[Category: | [[Category: Cha S-S]] | ||
[[Category: | [[Category: Jung HJ]] | ||
Latest revision as of 19:41, 1 November 2023
Graded expression of zinc-responsive genes through two regulatory zinc-binding sites in ZurGraded expression of zinc-responsive genes through two regulatory zinc-binding sites in Zur
Structural highlights
FunctionPublication Abstract from PubMedZinc is one of the essential transition metals in cells. Excess or lack of zinc is detrimental, and cells exploit highly sensitive zinc-binding regulators to achieve homeostasis. In this article, we present a crystal structure of active Zur from Streptomyces coelicolor with three zinc-binding sites (C-, M-, and D-sites). Mutations of the three sites differentially affected sporulation and transcription of target genes, such that C- and M-site mutations inhibited sporulation and derepressed all target genes examined, whereas D-site mutations did not affect sporulation and derepressed only a sensitive gene. Biochemical and spectroscopic analyses of representative metal site mutants revealed that the C-site serves a structural role, whereas the M- and D-sites regulate DNA-binding activity as an on-off switch and a fine-tuner, respectively. Consistent with differential effect of mutations on target genes, zinc chelation by TPEN derepressed some genes (znuA, rpmF2) more sensitively than others (rpmG2, SCO7682) in vivo. Similar pattern of TPEN-sensitivity was observed for Zur-DNA complexes formed on different promoters in vitro. The sensitive promoters bound Zur with lower affinity than the less sensitive ones. EDTA-treated apo-Zur gained its DNA binding activity at different concentrations of added zinc for the two promoter groups, corresponding to free zinc concentrations of 4.5x10(-16) M and 7.9x10(-16) M for the less sensitive and sensitive promoters, respectively. The graded expression of target genes is a clever outcome of subtly modulating Zur-DNA binding affinities in response to zinc availability. It enables bacteria to detect metal depletion with improved sensitivity and optimize gene-expression pattern. Graded expression of zinc-responsive genes through two regulatory zinc-binding sites in Zur.,Shin JH, Jung HJ, An YJ, Cho YB, Cha SS, Roe JH Proc Natl Acad Sci U S A. 2011 Mar 22;108(12):5045-50. Epub 2011 Mar 7. PMID:21383173[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|