4igl

From Proteopedia

(Difference between revisions)

Revision as of 20:43, 16 November 2022

Structure of the RHS-repeat containing BC component of the secreted ABC toxin complex from Yersinia entomophaga

Structural highlights

4igl is a 4 chain structure with sequence from Yersinia entomophaga. 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

YENB_YERET Part of an orally active toxin complex (TC) with strong insecticidal effects on larvae of the Coleoptera Costelytra zealandica, Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera larvae (PubMed:21278295, PubMed:22158901). The TC has an endochitinase activity (PubMed:21278295) (Probable).^[1] ^[2] ^[3]

Publication Abstract from PubMed

The ABC toxin complexes produced by certain bacteria are of interest owing to their potent insecticidal activity and potential role in human disease. These complexes comprise at least three proteins (A, B and C), which must assemble to be fully toxic. The carboxy-terminal region of the C protein is the main cytotoxic component, and is poorly conserved between different toxin complexes. A general model of action has been proposed, in which the toxin complex binds to the cell surface via the A protein, is endocytosed, and subsequently forms a pH-triggered channel, allowing the translocation of C into the cytoplasm, where it can cause cytoskeletal disruption in both insect and mammalian cells. Toxin complexes have been visualized using single-particle electron microscopy, but no high-resolution structures of the components are available, and the role of the B protein in the mechanism of toxicity remains unknown. Here we report the three-dimensional structure of the complex formed between the B and C proteins, determined to 2.5 A by X-ray crystallography. These proteins assemble to form an unprecedented, large hollow structure that encapsulates and sequesters the cytotoxic, C-terminal region of the C protein like the shell of an egg. The shell is decorated on one end by a beta-propeller domain, which mediates attachment of the B-C heterodimer to the A protein in the native complex. The structure reveals how C auto-proteolyses when folded in complex with B. The C protein is the first example, to our knowledge, of a structure that contains rearrangement hotspot (RHS) repeats, and illustrates a marked structural architecture that is probably conserved across both this widely distributed bacterial protein family and the related eukaryotic tyrosine-aspartate (YD)-repeat-containing protein family, which includes the teneurins. The structure provides the first clues about the function of these protein repeat families, and suggests a generic mechanism for protein encapsulation and delivery.

The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device.,Busby JN, Panjikar S, Landsberg MJ, Hurst MR, Lott JS Nature. 2013 Aug 4. doi: 10.1038/nature12465. PMID:23913273^[4]

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

References

↑ Hurst MR, Jones SA, Binglin T, Harper LA, Jackson TA, Glare TR. The main virulence determinant of Yersinia entomophaga MH96 is a broad-host-range toxin complex active against insects. J Bacteriol. 2011 Apr;193(8):1966-80. doi: 10.1128/JB.01044-10. Epub 2011 Jan 28. PMID:21278295 doi:http://dx.doi.org/10.1128/JB.01044-10
↑ Landsberg MJ, Jones SA, Rothnagel R, Busby JN, Marshall SD, Simpson RM, Lott JS, Hankamer B, Hurst MR. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20544-9. doi:, 10.1073/pnas.1111155108. Epub 2011 Dec 7. PMID:22158901 doi:http://dx.doi.org/10.1073/pnas.1111155108
↑ Landsberg MJ, Jones SA, Rothnagel R, Busby JN, Marshall SD, Simpson RM, Lott JS, Hankamer B, Hurst MR. 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity. Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):20544-9. doi:, 10.1073/pnas.1111155108. Epub 2011 Dec 7. PMID:22158901 doi:http://dx.doi.org/10.1073/pnas.1111155108
↑ Busby JN, Panjikar S, Landsberg MJ, Hurst MR, Lott JS. The BC component of ABC toxins is an RHS-repeat-containing protein encapsulation device. Nature. 2013 Aug 4. doi: 10.1038/nature12465. PMID:23913273 doi:10.1038/nature12465

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/4igl"

@@ Line 3: / Line 3: @@
 <StructureSection load='4igl' size='340' side='right'caption='[[4igl]], [[Resolution|resolution]] 2.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4igl]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IGL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IGL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4igl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_entomophaga Yersinia entomophaga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IGL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
+</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=K:POTASSIUM+ION'>K</scene></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=4igl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4igl OCA], [http://pdbe.org/4igl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4igl RCSB], [http://www.ebi.ac.uk/pdbsum/4igl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4igl ProSAT]</span></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=4igl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4igl OCA], [https://pdbe.org/4igl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4igl RCSB], [https://www.ebi.ac.uk/pdbsum/4igl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4igl ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/YENB_YERET YENB_YERET] Part of an orally active toxin complex (TC) with strong insecticidal effects on larvae of the Coleoptera Costelytra zealandica, Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera larvae (PubMed:21278295, PubMed:22158901). The TC has an endochitinase activity (PubMed:21278295) (Probable).<ref>PMID:21278295</ref> <ref>PMID:22158901</ref> <ref>PMID:22158901</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Busby, J N]]
+[[Category: Yersinia entomophaga]]
-[[Category: Hurst, M R.H]]
+[[Category: Busby JN]]
-[[Category: Landsberg, M J]]
+[[Category: Hurst MRH]]
-[[Category: Lott, J S]]
+[[Category: Landsberg MJ]]
-[[Category: Panjikar, S]]
+[[Category: Lott JS]]
-[[Category: Beta-propeller]]
+[[Category: Panjikar S]]
-[[Category: Rh]]
-[[Category: Secreted]]
-[[Category: Toxin]]
-[[Category: Toxin complex]]
-[[Category: Toxin transporter/chaperone]]

4igl

From Proteopedia

Revision as of 20:43, 16 November 2022

Structure of the RHS-repeat containing BC component of the secreted ABC toxin complex from Yersinia entomophaga

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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