3gz2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:46, 1 November 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3gz2.png|left|200px]]
 
-
<!--
+
==Crystal structure of IpgC in complex with an IpaB peptide==
-
The line below this paragraph, containing "STRUCTURE_3gz2", creates the "Structure Box" on the page.
+
<StructureSection load='3gz2' size='340' side='right'caption='[[3gz2]], [[Resolution|resolution]] 2.65&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'>[[3gz2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GZ2 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]] 2.65&#8491;</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=IMD:IMIDAZOLE'>IMD</scene></td></tr>
-
{{STRUCTURE_3gz2| PDB=3gz2 | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3gz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gz2 OCA], [https://pdbe.org/3gz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gz2 RCSB], [https://www.ebi.ac.uk/pdbsum/3gz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gz2 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/IPGC_SHIFL IPGC_SHIFL] Assists the correct folding of nascent IpaB. Once it is bound to IpaB, it binds to IpaC and impedes their premature association that would lead to their degradation in the absence of IpcG.
 +
== 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/gz/3gz2_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=3gz2 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Type III secretion systems (TTSSs) utilized by enteropathogenic bacteria require the presence of small, acidic virulence-associated chaperones for effective host cell infection. We adopted a combination of biochemical and cellular techniques to define the chaperone binding domains (CBDs) in the translocators IpaB and IpaC associated with the chaperone IpgC from Shigella flexneri. We identified a novel CBD in IpaB and furthermore precisely mapped the boundaries of the CBDs in both translocator proteins. In IpaC a single binding domain associates with IpgC. In IpaB, we show that the binding of the newly characterized CBD is essential in maintaining the ternary arrangement of chaperone-translocator complex. This hitherto unknown function is reflected in the co-crystal structure as well, with an IpgC dimer bound to an IpaB fragment comprising both CBDs. Moreover, in the absence of this novel CBD the IpaB/IpgC complex aggregates. This dual-recognition of a domain in the protein by the chaperone in facilitating the correct chaperone-substrate organization describes a new function for the TTSS associated chaperone-substrate complexes.
-
===Crystal structure of IpgC in complex with an IpaB peptide===
+
Combination of two separate binding domains defines stoichiometry between type III secretion system chaperone IpgC and translocator protein IpaB.,Lokareddy RK, Lunelli M, Eilers B, Wolter V, Kolbe M J Biol Chem. 2010 Dec 17;285(51):39965-75. Epub 2010 Oct 11. PMID:20937829<ref>PMID:20937829</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_20937829}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 3gz2" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 20937829 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_20937829}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
[[3gz2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GZ2 OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:20937829</ref><references group="xtra"/>
+
[[Category: Shigella flexneri]]
[[Category: Shigella flexneri]]
-
[[Category: Kolbe, M.]]
+
[[Category: Kolbe M]]
-
[[Category: Lokareddy, R K.]]
+
[[Category: Lokareddy RK]]
-
[[Category: Lunelli, M.]]
+
[[Category: Lunelli M]]

Current revision

Crystal structure of IpgC in complex with an IpaB peptide

PDB ID 3gz2

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools