1p5u

From Proteopedia

(Difference between revisions)

Current revision

X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex

Structural highlights

1p5u is a 3 chain structure with sequence from Yersinia pestis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.99Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CAF1M_YERPE Has a stimulatory role for the envelope antigen F1 secretion. It seems to interact with the subunit polypeptide and to prevent it from digestion by a protease.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation.

Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation.,Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, MacIntyre S, Knight SD Cell. 2003 May 30;113(5):587-96. PMID:12787500^[1]

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

References

↑ Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, MacIntyre S, Knight SD. Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation. Cell. 2003 May 30;113(5):587-96. PMID:12787500

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p5u"

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1p5u.png|left|200px]]
-<!--
+==X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex==
-The line below this paragraph, containing "STRUCTURE_1p5u", creates the "Structure Box" on the page.
+<StructureSection load='1p5u' size='340' side='right'caption='[[1p5u]], [[Resolution|resolution]] 1.99&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'>[[1p5u]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P5U 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]] 1.99&#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=1p5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p5u OCA], [https://pdbe.org/1p5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p5u RCSB], [https://www.ebi.ac.uk/pdbsum/1p5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p5u ProSAT]</span></td></tr>
-{{STRUCTURE_1p5u|  PDB=1p5u  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CAF1M_YERPE CAF1M_YERPE] Has a stimulatory role for the envelope antigen F1 secretion. It seems to interact with the subunit polypeptide and to prevent it from digestion by a protease.
+== 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/p5/1p5u_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1p5u ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation.
-===X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex===
+Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation.,Zavialov AV, Berglund J, Pudney AF, Fooks LJ, Ibrahim TM, MacIntyre S, Knight SD Cell. 2003 May 30;113(5):587-96. PMID:12787500<ref>PMID:12787500</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_12787500}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1p5u" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12787500 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_12787500}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-P5U is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P5U OCA].
-==Reference==
-<ref group="xtra">PMID:12787500</ref><references group="xtra"/>
 [[Category: Yersinia pestis]]
-[[Category: Berglund, J.]]
+[[Category: Berglund J]]
-[[Category: Fooks, L J.]]
+[[Category: Fooks LJ]]
-[[Category: Ibrahim, T M.]]
+[[Category: Ibrahim TM]]
-[[Category: Knight, S D.]]
+[[Category: Knight SD]]
-[[Category: MacIntyre, S.]]
+[[Category: MacIntyre S]]
-[[Category: Pudney, A F.]]
+[[Category: Pudney AF]]
-[[Category: Zavialov, A V.]]
+[[Category: Zavialov AV]]
-[[Category: Chaperone]]
-[[Category: Chaperone-subunit complex]]
-[[Category: Chaperone-target complex]]
-[[Category: Donor strand complementation]]
-[[Category: Donor strand exchange]]
-[[Category: Protein fiber]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:46:42 2009''

1p5u

From Proteopedia

Current revision

X-ray structure of the ternary Caf1M:Caf1:Caf1 chaperone:subunit:subunit complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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