1qpx: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='1qpx' size='340' side='right'caption='[[1qpx]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1qpx' size='340' side='right'caption='[[1qpx]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qpx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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> | </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> | </table> | ||
== Function == | == 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 32: | Line 31: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hultgren | [[Category: Hultgren SJ]] | ||
[[Category: Hung | [[Category: Hung DL]] | ||
[[Category: Knight | [[Category: Knight SD]] | ||
[[Category: Pinkner | [[Category: Pinkner JS]] | ||
Revision as of 12:49, 21 December 2022
CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERSCRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS
Structural highlights
FunctionPAPD_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 PubMedPapD 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 |
| ||||||||||||||