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==Solution structure of Pin1At from Arabidopsis thaliana==
==Solution structure of Pin1At from Arabidopsis thaliana==
<StructureSection load='1j6y' size='340' side='right'caption='[[1j6y]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1j6y' size='340' side='right'caption='[[1j6y]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1j6y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J6Y FirstGlance]. <br>
<table><tr><td colspan='2'>[[1j6y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J6Y FirstGlance]. <br>
</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=1j6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j6y OCA], [https://pdbe.org/1j6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j6y RCSB], [https://www.ebi.ac.uk/pdbsum/1j6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j6y ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1j6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j6y OCA], [https://pdbe.org/1j6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j6y RCSB], [https://www.ebi.ac.uk/pdbsum/1j6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j6y ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PIN1_ARATH PIN1_ARATH]] Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds.  
[https://www.uniprot.org/uniprot/PIN1_ARATH PIN1_ARATH] Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1j6y ConSurf].
</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=1j6y ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 119-amino acid residue prolyl cis/trans isomerase from Arabidopsis thaliana (PIN1At) is similar to the catalytic domain of the human hPIN1. However, PIN1At lacks the N-terminal WW domain that appears to be essential for the hPIN1 function. Here, the solution structure of PIN1At was determined by three-dimensional nuclear magnetic resonance spectroscopy. The PIN1At fold could be superimposed on that of the catalytic domain of hPIN1 and had a 19 residue flexible loop located between strand beta1 and helix alpha1. The dynamical features of this beta1/alpha1-loop, which are characteristic for a region involved in protein-protein interactions, led to exchange broadening in the NMR spectra. When sodium sulfate salt was added to the protein sample, the beta1/alpha1 loop was stabilized and, hence, a complete backbone resonance assignment was obtained. Previously, with a phospho-Cdc25 peptide as substrate, PIN1At had been shown to catalyze the phosphoserine/phosphothreonine prolyl cis/trans isomerization specifically. To map the catalytic site of PIN1At, the phospho-Cdc25 peptide or sodium sulfate salt was added in excess to the protein and chemical shift changes in the backbone amide protons were monitored in the (1)H(N)-(15)N heteronuclear single quantum coherence spectrum. The peptide caused perturbations in the loops between helix alpha4 and strand beta3, between strands beta3 and beta4, in the alpha3 helix, and in the beta1/alpha1 loop. The amide groups of the residues Arg21 and Arg22 showed large chemical shift perturbations upon phospho-Cdc25 peptide or sulfate addition. We conclude that this basic cluster formed by Arg21 and Arg22, both located in the beta1/alpha1 loop, is homologous to that found in the hPIN1 crystal structure (Arg68 and Arg69), which also is involved in sulfate ion binding. We showed that the sulfate group competed for the interaction between PIN1At and the phospho-Cdc25 peptide. In the absence of the WW domain, three hydrophobic residues (Ile33, Ile34, and Leu35) located in the long flexible loop and specific for the plant PIN-type peptidyl prolyl cis/trans isomerases (PPIases) could be an additional interaction site in PIN1At. However, phospho-peptide addition did not affect the resonances of these residues significantly. Electrostatic potential calculations revealed a negatively charged area not found in hPIN1 on the PIN1At molecular surface, which corresponds to the surface shielded by the WW domain in hPIN1. Based on our experimental results and the molecular specificities of the PIN1At enzyme, functional implications of the lack of WW domains in this plant PIN-type PPIase will be discussed.
Solution structure of the single-domain prolyl cis/trans isomerase PIN1At from Arabidopsis thaliana.,Landrieu I, Wieruszeski JM, Wintjens R, Inze D, Lippens G J Mol Biol. 2002 Jul 5;320(2):321-32. PMID:12079389<ref>PMID:12079389</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1j6y" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Arath]]
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Inze, D]]
[[Category: Inze D]]
[[Category: Landrieu, I]]
[[Category: Landrieu I]]
[[Category: Lippens, G]]
[[Category: Lippens G]]
[[Category: Wieruszeski, J M]]
[[Category: Wieruszeski JM]]
[[Category: Wintjens, R]]
[[Category: Wintjens R]]
[[Category: Isomerase]]
[[Category: Parvulin]]
[[Category: Phosphorylation]]
[[Category: Pin1]]
[[Category: Prolyl cis/trans isomerase]]

Revision as of 10:49, 3 April 2024

Solution structure of Pin1At from Arabidopsis thalianaSolution structure of Pin1At from Arabidopsis thaliana

Structural highlights

1j6y is a 1 chain structure with sequence from Arabidopsis thaliana. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PIN1_ARATH Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds.

Evolutionary Conservation

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

See Also

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