1qpx

From Proteopedia

(Difference between revisions)

Revision as of 09:49, 21 December 2022

CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS

Structural highlights

1qpx is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PAPD_ECOLX Binds and caps interactive surfaces on pilus subunits to prevent them from participating in non-productive interactions. Facilitates the import of subunits into the periplasm. May facilitate subunit folding. Chaperone-subunit complexes are then targeted to the PapC outer membrane usher where the chaperone must uncap from the subunits.

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

PapD is an immunoglobulin-like chaperone that mediates the assembly of P pili in uropathogenic strains of Escherichia coli. It binds and caps interactive surfaces on pilus subunits to prevent their premature associations in the periplasm. We elucidated the structural basis of a mechanism whereby PapD also interacts with itself, capping its own subunit binding surface. Crystal structures of dimeric forms of PapD revealed that this self-capping mechanism involves a rearrangement and ordering of the C2-D2 and F1-G1 loops upon dimerization which might ensure that a stable dimer is not formed in solution in spite of a relatively large dimer interface. An analysis of site directed mutations revealed that chaperone dimerization requires the same surface that is otherwise used to bind subunits.

Structural basis of chaperone self-capping in P pilus biogenesis.,Hung DL, Pinkner JS, Knight SD, Hultgren SJ Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):8178-83. PMID:10393968^[1]

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

References

↑ Hung DL, Pinkner JS, Knight SD, Hultgren SJ. Structural basis of chaperone self-capping in P pilus biogenesis. Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):8178-83. PMID:10393968

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/1qpx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1qpx' size='340' side='right'caption='[[1qpx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qpx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QPX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qpx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QPX FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dpa|3dpa]], [[1qpp|1qpp]]</div></td></tr>
+</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=1qpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpx OCA], [https://pdbe.org/1qpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qpx RCSB], [https://www.ebi.ac.uk/pdbsum/1qpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qpx 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=1qpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpx OCA], [https://pdbe.org/1qpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qpx RCSB], [https://www.ebi.ac.uk/pdbsum/1qpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qpx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/PAPD_ECOLX PAPD_ECOLX]] Binds and caps interactive surfaces on pilus subunits to prevent them from participating in non-productive interactions. Facilitates the import of subunits into the periplasm. May facilitate subunit folding. Chaperone-subunit complexes are then targeted to the PapC outer membrane usher where the chaperone must uncap from the subunits.
+[https://www.uniprot.org/uniprot/PAPD_ECOLX PAPD_ECOLX] Binds and caps interactive surfaces on pilus subunits to prevent them from participating in non-productive interactions. Facilitates the import of subunits into the periplasm. May facilitate subunit folding. Chaperone-subunit complexes are then targeted to the PapC outer membrane usher where the chaperone must uncap from the subunits.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 31: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Hultgren, S J]]
+[[Category: Hultgren SJ]]
-[[Category: Hung, D L]]
+[[Category: Hung DL]]
-[[Category: Knight, S D]]
+[[Category: Knight SD]]
-[[Category: Pinkner, J S]]
+[[Category: Pinkner JS]]
-[[Category: Beta barrel]]
-[[Category: Chaperone]]
-[[Category: Immunoglobulin fold]]

1qpx

From Proteopedia

Revision as of 09:49, 21 December 2022

CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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