1tqq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:33, 23 August 2023) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1tqq.png|left|200px]]
 
-
<!--
+
==Structure of TolC in complex with hexamminecobalt==
-
The line below this paragraph, containing "STRUCTURE_1tqq", creates the "Structure Box" on the page.
+
<StructureSection load='1tqq' size='340' side='right'caption='[[1tqq]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1tqq]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TQQ FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene></td></tr>
-
{{STRUCTURE_1tqq| PDB=1tqq | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tqq OCA], [https://pdbe.org/1tqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tqq RCSB], [https://www.ebi.ac.uk/pdbsum/1tqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tqq ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TOLC_ECOLI TOLC_ECOLI] Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells.<ref>PMID:6337123</ref> <ref>PMID:11274125</ref> <ref>PMID:15228545</ref> <ref>PMID:18955484</ref> <ref>PMID:23176499</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tq/1tqq_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1tqq ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The trimeric TolC protein of Escherichia coli comprises an outer membrane beta-barrel and a contiguous alpha-helical barrel projecting across the periplasm. This provides a single 140 A long pore for multidrug efflux and protein export. We have previously reported that trivalent cations such as hexammine cobalt can severely inhibit the conductivity of the TolC pore reconstituted in planar lipid bilayers. Here, isothermal calorimetry shows that Co(NH(3))(6)(3+) binds to TolC with an affinity of 20 nM. The crystal structure of the TolC-Co(NH(3))(6)(3+) complex was determined to 2.75 A resolution, and showed no significant difference in the protein when compared with unliganded TolC. An electron density difference map revealed that a single ligand molecule binds at the centre of the periplasmic entrance, the sole constriction of TolC. The octahedral symmetry of the ligand and the three-fold rotational symmetry of the TolC entrance determine a binding site in which the ligand forms hydrogen bonds with the Asp(374) residue of each monomer. When Asp(374) was substituted by alanine, high affinity ligand binding was abolished and inhibition of TolC pore conductivity in lipid bilayers was alleviated. Comparable effects followed independent substitution of the neighbouring Asp(371), indicating that this aspartate ring also contributes to the high affinity ligand binding site. As the electronegative entrance is widely conserved in the TolC family, it may be a useful target for the development of inhibitors against multidrug resistant pathogenic bacteria.
-
===Structure of TolC in complex with hexamminecobalt===
+
Structure of the ligand-blocked periplasmic entrance of the bacterial multidrug efflux protein TolC.,Higgins MK, Eswaran J, Edwards P, Schertler GF, Hughes C, Koronakis V J Mol Biol. 2004 Sep 17;342(3):697-702. PMID:15342230<ref>PMID:15342230</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_15342230}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1tqq" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 15342230 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_15342230}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1TQQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TQQ OCA].
+
-
 
+
-
==Reference==
+
-
Structure of the ligand-blocked periplasmic entrance of the bacterial multidrug efflux protein TolC., Higgins MK, Eswaran J, Edwards P, Schertler GF, Hughes C, Koronakis V, J Mol Biol. 2004 Sep 17;342(3):697-702. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15342230 15342230]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Edwards, P C.]]
+
[[Category: Edwards PC]]
-
[[Category: Eswaran, J.]]
+
[[Category: Eswaran J]]
-
[[Category: Higgins, M K.]]
+
[[Category: Higgins MK]]
-
[[Category: Hughes, C.]]
+
[[Category: Hughes C]]
-
[[Category: Koronakis, V.]]
+
[[Category: Koronakis V]]
-
[[Category: Schertler, G F.]]
+
[[Category: Schertler GF]]
-
[[Category: Alpha-barrel]]
+
-
[[Category: Beta-barrel]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 05:43:39 2008''
+

Current revision

Structure of TolC in complex with hexamminecobalt

PDB ID 1tqq

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1tqq"
Personal tools