3tlq

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of EAL-like domain protein YdiV

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3tlq"

@@ Line 3: / Line 3: @@
 <StructureSection load='3tlq' size='340' side='right'caption='[[3tlq]], [[Resolution|resolution]] 1.91&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3tlq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TLQ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3tlq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TLQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TLQ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.91&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4es4|4es4]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b1707, JW1697, ydiV ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=3tlq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tlq OCA], [https://pdbe.org/3tlq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tlq RCSB], [https://www.ebi.ac.uk/pdbsum/3tlq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tlq ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/YDIV_ECOLI YDIV_ECOLI]] Upon overexpression acts as a novel anti-FlhC(2)FlhD(4) factor, decreasing its DNA-binding activity, able to negatively regulate expression of flagellar class II operons including FliC.<ref>PMID:22461489</ref>
+[https://www.uniprot.org/uniprot/YDIV_ECOLI YDIV_ECOLI] Upon overexpression acts as a novel anti-FlhC(2)FlhD(4) factor, decreasing its DNA-binding activity, able to negatively regulate expression of flagellar class II operons including FliC.<ref>PMID:22461489</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-YdiV is a negative regulator of cell motility. It interacts with FlhD(4)C(2) complex, a product of flagellar master operon, which works as the transcription activator of all other flagellar operons. Here, we report the crystal structures of YdiV and YdiV(2)-FlhD(2) complex at 1.9 A and 2.9 A resolutions, respectively. Interestingly, YdiV formed multiple types of complexes with FlhD(4)C(2). YdiV(1)-FlhD(4)C(2) and YdiV(2)-FlhD(4)C(2) still bound to DNA, while YdiV(3)-FlhD(4)C(2) and YdiV(4)-FlhD(4)C(2) did not. DNA bound FlhD(4)C(2) through wrapping around the FlhC subunit rather than the FlhD subunit. Structural analysis showed that only two peripheral FlhD subunits were accessible for YdiV binding, forming the YdiV(2)-FlhD(4)C(2) complex without affecting the integrity of ring-like structure. YdiV(2)-FlhD(2) structure and the negative staining electron microscopy reconstruction of YdiV(4)-FlhD(4)C(2) suggested that the third and fourth YdiV molecule bound to the FlhD(4)C(2) complex through squeezing into the ring-like structure of FlhD(4)C(2) between the two internal D subunits. Consequently, the ring-like structure opened up, and the complex lost DNA-binding ability. Thus, YdiV inhibits FlhD(4)C(2) only at relatively high concentrations.
-Structural insight of a concentration-dependent mechanism by which YdiV inhibits Escherichia coli flagellum biogenesis and motility.,Li B, Li N, Wang F, Guo L, Huang Y, Liu X, Wei T, Zhu D, Liu C, Pan H, Xu S, Wang HW, Gu L Nucleic Acids Res. 2012 Sep 21. PMID:23002140<ref>PMID:23002140</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3tlq" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Gu, L]]
+[[Category: Gu L]]
-[[Category: Guo, L]]
+[[Category: Guo L]]
-[[Category: Li, B]]
+[[Category: Li B]]
-[[Category: Li, N]]
+[[Category: Li N]]
-[[Category: Liu, C]]
+[[Category: Liu C]]
-[[Category: Wang, F]]
+[[Category: Wang F]]
-[[Category: Xu, S]]
+[[Category: Xu S]]
-[[Category: Zhu, D]]
+[[Category: Zhu D]]
-[[Category: Anti-flhd4c2 factor]]
-[[Category: Repress motility]]
-[[Category: Transcription]]

3tlq

From Proteopedia

Current revision

Crystal structure of EAL-like domain protein YdiV

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox