This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2rqs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:06, 1 May 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==3D structure of Pin from the psychrophilic archeon Cenarcheaum symbiosum (CsPin)==
==3D structure of Pin from the psychrophilic archeon Cenarcheaum symbiosum (CsPin)==
-
<StructureSection load='2rqs' size='340' side='right'caption='[[2rqs]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+
<StructureSection load='2rqs' size='340' side='right'caption='[[2rqs]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2rqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"cenarchaeum_symbiosum"_delong_and_preston_1996 "cenarchaeum symbiosum" delong and preston 1996]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RQS FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2rqs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cenarchaeum_symbiosum Cenarchaeum symbiosum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RQS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RQS FirstGlance]. <br>
-
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pinA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=46770 "Cenarchaeum symbiosum" DeLong and Preston 1996])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=2rqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rqs OCA], [https://pdbe.org/2rqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rqs RCSB], [https://www.ebi.ac.uk/pdbsum/2rqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rqs 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=2rqs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rqs OCA], [https://pdbe.org/2rqs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rqs RCSB], [https://www.ebi.ac.uk/pdbsum/2rqs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rqs ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/O74049_CENSY O74049_CENSY]
-
Parvulins are a group of peptidyl-prolyl isomerases (PPIases) responsible for important biological processes in all kingdoms of life. The PinA protein from the psychrophilic archaeon Cenarchaeum symbiosum is a parvulin-like PPIase. Due to its striking similarity to the human parvulins Pin1 and Par14, PinA constitutes an interesting subject for structural and functional studies. Here, we present the first high resolution NMR structure of an archaeal parvulin, PinA, based on 1798 conformational restraints. Structure calculation yields an ensemble of 20 convergent low energy structures with a backbone r.m.s.d. value of 0.6 A within the secondary structure elements. The overall fold of PinA comprises the beta-alpha(3)-beta-alpha-beta(2) fold typical for all parvulin structures known so far, but with helix III being a short 3(10)-helix. A detailed comparison of this high resolution structure of the first archaeal PinA protein with bacterial and eukaryotic parvulin PPIase structures reveals an atypically large catalytic binding site. This feature provides an explanation for cold-adapted protein function. Moreover, the residues in and around 3(10)-helix III exhibit strong intramolecular dynamics on a microsecond to millisecond timescale and display structural heterogeneity within the NMR ensemble. A putative peptide ligand was found for PinA by phage display and was used for (1)H-(15)N-HSQC titrations. Again, the flexible region around 3(10)-helix III as well as residues of the peptide binding pocket showed the strongest chemical shift perturbations upon peptide binding. The local flexibility of this region also was modulated by ligand binding. A glycine and two positively charged residues are conserved in most parvulin proteins in this flexible loop region, which may be of general functional importance for parvulin-type PPIases.
+
-
 
+
-
Structure and Dynamics of the First Archaeal Parvulin Reveal a New Functionally Important Loop in Parvulin-type Prolyl Isomerases.,Jaremko L, Jaremko M, Elfaki I, Mueller JW, Ejchart A, Bayer P, Zhukov I J Biol Chem. 2011 Feb 25;286(8):6554-65. Epub 2010 Dec 7. PMID:21138844<ref>PMID:21138844</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 2rqs" 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: Cenarchaeum symbiosum delong and preston 1996]]
+
[[Category: Cenarchaeum symbiosum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Peptidylprolyl isomerase]]
+
[[Category: Bayer P]]
-
[[Category: Bayer, P]]
+
[[Category: Jaremko L]]
-
[[Category: Jaremko, L]]
+
[[Category: Jaremko M]]
-
[[Category: Jaremko, M]]
+
[[Category: Mueller JW]]
-
[[Category: Mueller, J W]]
+
[[Category: Zhukov I]]
-
[[Category: Zhukov, I]]
+
-
[[Category: Cell cycle]]
+
-
[[Category: Cenarcheaum symbiosum]]
+
-
[[Category: Cis/trans isomerisation]]
+
-
[[Category: Isomerase]]
+
-
[[Category: Low temperature]]
+
-
[[Category: Nima-kinase]]
+
-
[[Category: Parvulin]]
+
-
[[Category: Pin1]]
+

Current revision

3D structure of Pin from the psychrophilic archeon Cenarcheaum symbiosum (CsPin)

PDB ID 2rqs

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rqs"
Personal tools