3pcs: Difference between revisions

Latest revision as of 09:51, 6 September 2023

Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex

Structural highlights

3pcs is a 8 chain structure with sequence from Escherichia coli O157:H7 and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.86Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q7DB50_ECO57

Publication Abstract from PubMed

The fidelity and specificity of information flow within a cell is controlled by scaffolding proteins that assemble and link enzymes into signalling circuits. These circuits can be inhibited by bacterial effector proteins that post-translationally modify individual pathway components. However, there is emerging evidence that pathogens directly organize higher-order signalling networks through enzyme scaffolding, and the identity of the effectors and their mechanisms of action are poorly understood. Here we identify the enterohaemorrhagic Escherichia coli O157:H7 type III effector EspG as a regulator of endomembrane trafficking using a functional screen, and report ADP-ribosylation factor (ARF) GTPases and p21-activated kinases (PAKs) as its relevant host substrates. The 2.5 A crystal structure of EspG in complex with ARF6 shows how EspG blocks GTPase-activating-protein-assisted GTP hydrolysis, revealing a potent mechanism of GTPase signalling inhibition at organelle membranes. In addition, the 2.8 A crystal structure of EspG in complex with the autoinhibitory Ialpha3-helix of PAK2 defines a previously unknown catalytic site in EspG and provides an allosteric mechanism of kinase activation by a bacterial effector. Unexpectedly, ARF and PAKs are organized on adjacent surfaces of EspG, indicating its role as a 'catalytic scaffold' that effectively reprograms cellular events through the functional assembly of GTPase-kinase signalling complex.

The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold.,Selyunin AS, Sutton SE, Weigele BA, Reddick LE, Orchard RC, Bresson SM, Tomchick DR, Alto NM Nature. 2010 Dec 19. PMID:21170023^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Selyunin AS, Sutton SE, Weigele BA, Reddick LE, Orchard RC, Bresson SM, Tomchick DR, Alto NM. The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold. Nature. 2010 Dec 19. PMID:21170023 doi:10.1038/nature09593

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OCA

[1] Selyunin AS, Sutton SE, Weigele BA, Reddick LE, Orchard RC, Bresson SM, Tomchick DR, Alto NM. The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold. Nature. 2010 Dec 19. PMID:21170023 doi:10.1038/nature09593

[1]

@@ Line 1: / Line 1: @@
-[[Image:3pcs.jpg|left|200px]]
-<!--
+==Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex==
-The line below this paragraph, containing "STRUCTURE_3pcs", creates the "Structure Box" on the page.
+<StructureSection load='3pcs' size='340' side='right'caption='[[3pcs]], [[Resolution|resolution]] 2.86&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'>[[3pcs]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PCS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PCS 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]] 2.86&#8491;</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=3pcs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pcs OCA], [https://pdbe.org/3pcs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pcs RCSB], [https://www.ebi.ac.uk/pdbsum/3pcs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pcs ProSAT]</span></td></tr>
-{{STRUCTURE_3pcs|  PDB=3pcs  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q7DB50_ECO57 Q7DB50_ECO57]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The fidelity and specificity of information flow within a cell is controlled by scaffolding proteins that assemble and link enzymes into signalling circuits. These circuits can be inhibited by bacterial effector proteins that post-translationally modify individual pathway components. However, there is emerging evidence that pathogens directly organize higher-order signalling networks through enzyme scaffolding, and the identity of the effectors and their mechanisms of action are poorly understood. Here we identify the enterohaemorrhagic Escherichia coli O157:H7 type III effector EspG as a regulator of endomembrane trafficking using a functional screen, and report ADP-ribosylation factor (ARF) GTPases and p21-activated kinases (PAKs) as its relevant host substrates. The 2.5 A crystal structure of EspG in complex with ARF6 shows how EspG blocks GTPase-activating-protein-assisted GTP hydrolysis, revealing a potent mechanism of GTPase signalling inhibition at organelle membranes. In addition, the 2.8 A crystal structure of EspG in complex with the autoinhibitory Ialpha3-helix of PAK2 defines a previously unknown catalytic site in EspG and provides an allosteric mechanism of kinase activation by a bacterial effector. Unexpectedly, ARF and PAKs are organized on adjacent surfaces of EspG, indicating its role as a 'catalytic scaffold' that effectively reprograms cellular events through the functional assembly of GTPase-kinase signalling complex.
-===Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex===
+The assembly of a GTPase-kinase signalling complex by a bacterial catalytic scaffold.,Selyunin AS, Sutton SE, Weigele BA, Reddick LE, Orchard RC, Bresson SM, Tomchick DR, Alto NM Nature. 2010 Dec 19. PMID:21170023<ref>PMID:21170023</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_21170023}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3pcs" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 21170023 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_21170023}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Escherichia coli O157:H7]]
-[[3pcs]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PCS OCA].
-==Reference==
-<ref group="xtra">PMID:21170023</ref><references group="xtra"/>
-[[Category: Escherichia coli o157:h7]]
 [[Category: Homo sapiens]]
-[[Category: Non-specific serine/threonine protein kinase]]
+[[Category: Large Structures]]
-[[Category: Alto, N M.]]
+[[Category: Alto NM]]
-[[Category: Selyunin, A S.]]
+[[Category: Selyunin AS]]
-[[Category: Tomchick, D R.]]
+[[Category: Tomchick DR]]

3pcs: Difference between revisions

Latest revision as of 09:51, 6 September 2023

Structure of EspG-PAK2 autoinhibitory Ialpha3 helix complex

Structural highlights

Function

Publication Abstract from PubMed

References

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