4rtd

From Proteopedia

(Difference between revisions)

Revision as of 08:27, 8 March 2023

Escherichia coli alpha-2-macroglobulin activated by porcine elastase

Structural highlights

4rtd is a 1 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A2MG_ECOLI Protects the bacterial cell from host peptidases (PubMed:18697741, PubMed:26143919, PubMed:26100869). Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase (PubMed:26143919, PubMed:26100869). Trapped peptidases are still active except against very large substrates (PubMed:26100869). May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases (PubMed:26100869).^[1] ^[2] ^[3]

Publication Abstract from PubMed

Bacterial alpha-2-macroglobulins have been suggested to function in defence as broad-spectrum inhibitors of host proteases that breach the outer membrane. Here, the X-ray structure of protease-cleaved Escherichia coli alpha-2-macroglobulin is described, which reveals a putative mechanism of activation and conformational change essential for protease inhibition. In this competitive mechanism, protease cleavage of the bait-region domain results in the untethering of an intrinsically disordered region of this domain which disrupts native interdomain interactions that maintain E. coli alpha-2-macroglobulin in the inactivated form. The resulting global conformational change results in entrapment of the protease and activation of the thioester bond that covalently links to the attacking protease. Owing to the similarity in structure and domain architecture of Escherichia coli alpha-2-macroglobulin and human alpha-2-macroglobulin, this protease-activation mechanism is likely to operate across the diverse members of this group.

Structure of protease-cleaved Escherichia coli alpha-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment.,Fyfe CD, Grinter R, Josts I, Mosbahi K, Roszak AW, Cogdell RJ, Wall DM, Burchmore RJ, Byron O, Walker D Acta Crystallogr D Biol Crystallogr. 2015 Jul 1;71(Pt 7):1478-86. doi:, 10.1107/S1399004715008548. Epub 2015 Jun 30. PMID:26143919^[4]

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

References

↑ Doan N, Gettins PG. alpha-Macroglobulins are present in some gram-negative bacteria: characterization of the alpha2-macroglobulin from Escherichia coli. J Biol Chem. 2008 Oct 17;283(42):28747-56. PMID:18697741 doi:10.1074/jbc.M803127200
↑ Garcia-Ferrer I, Arede P, Gomez-Blanco J, Luque D, Duquerroy S, Caston JR, Goulas T, Gomis-Ruth FX. Structural and functional insights into Escherichia coli alpha2-macroglobulin endopeptidase snap-trap inhibition. Proc Natl Acad Sci U S A. 2015 Jun 22. pii: 201506538. PMID:26100869 doi:http://dx.doi.org/10.1073/pnas.1506538112
↑ Fyfe CD, Grinter R, Josts I, Mosbahi K, Roszak AW, Cogdell RJ, Wall DM, Burchmore RJ, Byron O, Walker D. Structure of protease-cleaved Escherichia coli alpha-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment. Acta Crystallogr D Biol Crystallogr. 2015 Jul 1;71(Pt 7):1478-86. doi:, 10.1107/S1399004715008548. Epub 2015 Jun 30. PMID:26143919 doi:http://dx.doi.org/10.1107/S1399004715008548
↑ Fyfe CD, Grinter R, Josts I, Mosbahi K, Roszak AW, Cogdell RJ, Wall DM, Burchmore RJ, Byron O, Walker D. Structure of protease-cleaved Escherichia coli alpha-2-macroglobulin reveals a putative mechanism of conformational activation for protease entrapment. Acta Crystallogr D Biol Crystallogr. 2015 Jul 1;71(Pt 7):1478-86. doi:, 10.1107/S1399004715008548. Epub 2015 Jun 30. PMID:26143919 doi:http://dx.doi.org/10.1107/S1399004715008548

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4rtd"

@@ Line 3: / Line 3: @@
 <StructureSection load='4rtd' size='340' side='right'caption='[[4rtd]], [[Resolution|resolution]] 3.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4rtd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RTD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RTD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4rtd]] is a 1 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=4RTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RTD FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4u48|4u48]], [[4u59|4u59]], [[4acq|4acq]]</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=4rtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rtd OCA], [https://pdbe.org/4rtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rtd RCSB], [https://www.ebi.ac.uk/pdbsum/4rtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rtd ProSAT]</span></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b2520, JW2504, yfhM ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rtd OCA], [http://pdbe.org/4rtd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rtd RCSB], [http://www.ebi.ac.uk/pdbsum/4rtd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rtd ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/A2MG_ECOLI A2MG_ECOLI] Protects the bacterial cell from host peptidases (PubMed:18697741, PubMed:26143919, PubMed:26100869). Acts by a 'trapping' mechanism. Cleavage of the bait-region domain by host peptidases leads to a global conformational change, which results in entrapment of the host peptidase and activation of the thioester bond that covalently binds the attacking host peptidase (PubMed:26143919, PubMed:26100869). Trapped peptidases are still active except against very large substrates (PubMed:26100869). May protect the entire periplam, including the lipoproteins anchored to the periplasmic side of the outer membrane, against intruding endopeptidases (PubMed:26100869).<ref>PMID:18697741</ref> <ref>PMID:26100869</ref> <ref>PMID:26143919</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Cogdell, R J]]
+[[Category: Cogdell RJ]]
-[[Category: Fyfe, C D]]
+[[Category: Fyfe CD]]
-[[Category: Grinter, R]]
+[[Category: Grinter R]]
-[[Category: Josts, I]]
+[[Category: Josts I]]
-[[Category: Roszak, A W]]
+[[Category: Roszak AW]]
-[[Category: Walker, D]]
+[[Category: Walker D]]
-[[Category: Lipid binding protein]]
-[[Category: Macroglobulin]]
-[[Category: Thioester domain]]

4rtd

From Proteopedia

Revision as of 08:27, 8 March 2023

Escherichia coli alpha-2-macroglobulin activated by porcine elastase

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox