1pan: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1pan.gif|left|200px]]


{{Structure
==A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN==
|PDB= 1pan |SIZE=350|CAPTION= <scene name='initialview01'>1pan</scene>
<StructureSection load='1pan' size='340' side='right'caption='[[1pan]]' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
<table><tr><td colspan='2'>[[1pan]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PAN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PAN FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></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=1pan FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pan OCA], [https://pdbe.org/1pan PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pan RCSB], [https://www.ebi.ac.uk/pdbsum/1pan PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pan ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PILA_PSEAE PILA_PSEAE] Major component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (PubMed:26041805, PubMed:31431558, PubMed:9282737). In addition, plays a critical role in type II secretion of exoenzymes by interacting with specific components such as XcpT or XcpU (PubMed:9282737). Modulates host calcium signaling through interaction with host calcium-modulating cyclophilin ligand (PubMed:23266901).<ref>PMID:23266901</ref> <ref>PMID:26041805</ref> <ref>PMID:31431558</ref> <ref>PMID:9282737</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structures of peptide antigens from the receptor binding domains of Pseudomonas aeruginosa strains PAO and KB7 have been determined using two-dimensional 1H NMR techniques. Ensembles of solution conformations for the trans forms of these 17-residue disulfide-bridged peptides have been generated using a simulated annealing procedure in conjunction with distance and torsion angle restraints derived from NMR data. Comparison of the NMR-derived solution structures of the PAO and KB7 peptides, with that previously determined (McInnes et al., 1993) and herein refined for the PAK peptide reveals a common structural motif. All three peptide structures contain a type I beta-turn in the conserved sequence Asp134-X-X-Phe137 and a type II beta-turn in the conserved sequence Pro139-X-Gly-Cys142. However, the overall folds of the three peptides differ as well as the disposition of the side chains comprising the hydrophobic pockets. The similarities and differences between the structures of the three strains which bind to a common cell surface receptor are discussed in light of their contributions to synthetic vaccine design.


'''A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN'''
Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design.,Campbell AP, McInnes C, Hodges RS, Sykes BD Biochemistry. 1995 Dec 19;34(50):16255-68. PMID:8845350<ref>PMID:8845350</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1pan" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The solution structures of peptide antigens from the receptor binding domains of Pseudomonas aeruginosa strains PAO and KB7 have been determined using two-dimensional 1H NMR techniques. Ensembles of solution conformations for the trans forms of these 17-residue disulfide-bridged peptides have been generated using a simulated annealing procedure in conjunction with distance and torsion angle restraints derived from NMR data. Comparison of the NMR-derived solution structures of the PAO and KB7 peptides, with that previously determined (McInnes et al., 1993) and herein refined for the PAK peptide reveals a common structural motif. All three peptide structures contain a type I beta-turn in the conserved sequence Asp134-X-X-Phe137 and a type II beta-turn in the conserved sequence Pro139-X-Gly-Cys142. However, the overall folds of the three peptides differ as well as the disposition of the side chains comprising the hydrophobic pockets. The similarities and differences between the structures of the three strains which bind to a common cell surface receptor are discussed in light of their contributions to synthetic vaccine design.
*[[Pilin 3D structures|Pilin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1PAN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PAN OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design., Campbell AP, McInnes C, Hodges RS, Sykes BD, Biochemistry. 1995 Dec 19;34(50):16255-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8845350 8845350]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Campbell AP]]
[[Category: Campbell, A P.]]
[[Category: Hodges RS]]
[[Category: Hodges, R S.]]
[[Category: Mcinnes C]]
[[Category: Mcinnes, C.]]
[[Category: Sykes BD]]
[[Category: Sykes, B D.]]
[[Category: ACE]]
[[Category: fimbrial protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:01 2008''

Latest revision as of 10:12, 30 October 2024

A COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGNA COMPARISON OF NMR SOLUTION STRUCTURES OF THE RECEPTOR BINDING DOMAINS OF PSEUDOMONAS AERUGINOSA PILI STRAINS PAO, KB7, AND PAK: IMPLICATIONS FOR RECEPTOR BINDING AND SYNTHETIC VACCINE DESIGN

Structural highlights

1pan is a 1 chain structure with sequence from Pseudomonas aeruginosa. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 1 model
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PILA_PSEAE Major component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers (PubMed:26041805, PubMed:31431558, PubMed:9282737). In addition, plays a critical role in type II secretion of exoenzymes by interacting with specific components such as XcpT or XcpU (PubMed:9282737). Modulates host calcium signaling through interaction with host calcium-modulating cyclophilin ligand (PubMed:23266901).[1] [2] [3] [4]

Publication Abstract from PubMed

The solution structures of peptide antigens from the receptor binding domains of Pseudomonas aeruginosa strains PAO and KB7 have been determined using two-dimensional 1H NMR techniques. Ensembles of solution conformations for the trans forms of these 17-residue disulfide-bridged peptides have been generated using a simulated annealing procedure in conjunction with distance and torsion angle restraints derived from NMR data. Comparison of the NMR-derived solution structures of the PAO and KB7 peptides, with that previously determined (McInnes et al., 1993) and herein refined for the PAK peptide reveals a common structural motif. All three peptide structures contain a type I beta-turn in the conserved sequence Asp134-X-X-Phe137 and a type II beta-turn in the conserved sequence Pro139-X-Gly-Cys142. However, the overall folds of the three peptides differ as well as the disposition of the side chains comprising the hydrophobic pockets. The similarities and differences between the structures of the three strains which bind to a common cell surface receptor are discussed in light of their contributions to synthetic vaccine design.

Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design.,Campbell AP, McInnes C, Hodges RS, Sykes BD Biochemistry. 1995 Dec 19;34(50):16255-68. PMID:8845350[5]

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

See Also

References

  1. ↑ Okuda J, Hayashi N, Arakawa M, Minagawa S, Gotoh N. Type IV pilus protein PilA of Pseudomonas aeruginosa modulates calcium signaling through binding the calcium-modulating cyclophilin ligand. J Infect Chemother. 2013 Aug;19(4):653-64. PMID:23266901 doi:10.1007/s10156-012-0536-y
  2. ↑ Persat A, Inclan YF, Engel JN, Stone HA, Gitai Z. Type IV pili mechanochemically regulate virulence factors in Pseudomonas aeruginosa. Proc Natl Acad Sci U S A. 2015 Jun 16;112(24):7563-8. PMID:26041805 doi:10.1073/pnas.1502025112
  3. ↑ Nieto V, Kroken AR, Grosser MR, Smith BE, Metruccio MME, Hagan P, Hallsten ME, Evans DJ, Fleiszig SMJ. Type IV Pili Can Mediate Bacterial Motility within Epithelial Cells. mBio. 2019 Aug 20;10(4):e02880-18. PMID:31431558 doi:10.1128/mBio.02880-18
  4. ↑ Lu HM, Motley ST, Lory S. Interactions of the components of the general secretion pathway: role of Pseudomonas aeruginosa type IV pilin subunits in complex formation and extracellular protein secretion. Mol Microbiol. 1997 Jul;25(2):247-59. PMID:9282737 doi:10.1046/j.1365-2958.1997.4561818.x
  5. ↑ Campbell AP, McInnes C, Hodges RS, Sykes BD. Comparison of NMR solution structures of the receptor binding domains of Pseudomonas aeruginosa pili strains PAO, KB7, and PAK: implications for receptor binding and synthetic vaccine design. Biochemistry. 1995 Dec 19;34(50):16255-68. PMID:8845350
Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1pan&oldid=4200116"