View source for 4yuj


==Multiconformer synchrotron model of CypA at 240 K==
<StructureSection load='4yuj' size='340' side='right'caption='[[4yuj]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yuj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YUJ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.42&#8491;</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=4yuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yuj OCA], [https://pdbe.org/4yuj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yuj RCSB], [https://www.ebi.ac.uk/pdbsum/4yuj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yuj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Determining the interconverting conformations of dynamic proteins in atomic detail is a major challenge for structural biology. Conformational heterogeneity in the active site of the dynamic enzyme cyclophilin A (CypA) has been previously linked to its catalytic function, but the extent to which the different conformations of these residues are correlated is unclear. We monitored the temperature dependences of these alternative conformations with eight synchrotron datasets spanning 100-310 K. Multiconformer models show that many alternative conformations in CypA are populated only at 240 K and above, yet others remain populated or become populated at 180 K and below. These results point to a complex evolution of conformational heterogeneity between 180-240 K that involves both thermal deactivation and solvent-driven arrest of protein motions in the crystal. Together, our multitemperature analyses and XFEL data motivate a new generation of temperature- and time-resolved experiments to structurally characterize the dynamic underpinnings of protein function.

.,Keedy DA, Kenner LR, Warkentin M, Woldeyes RA, Hopkins JB, Thompson MC, Brewster AS, Van Benschoten AH, Baxter EL, Uervirojnangkoorn M, McPhillips SE, Song J, Alonso-Mori R, Holton JM, Weis WI, Brunger AT, Soltis SM, Lemke H, Gonzalez A, Sauter NK, Cohen AE, van den Bedem H, Thorne RE, Fraser JS Elife. 2015 Sep 30;4. doi: 10.7554/eLife.07574. PMID:26422513<ref>PMID:26422513</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yuj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Baxter EL]]
[[Category: Brewster AS]]
[[Category: Brunger AT]]
[[Category: Cohen AE]]
[[Category: Fraser JS]]
[[Category: Gonzalez A]]
[[Category: Holton JM]]
[[Category: Hopkins JB]]
[[Category: Keedy DA]]
[[Category: Kenner LR]]
[[Category: Lemke H]]
[[Category: McPhillips SE]]
[[Category: Mori RA]]
[[Category: Sauter NK]]
[[Category: Soltis M]]
[[Category: Song J]]
[[Category: Thompson MC]]
[[Category: Thorne RE]]
[[Category: Uervirojnangkoorn M]]
[[Category: Van Benschoten AH]]
[[Category: Warkentin M]]
[[Category: Weis WI]]
[[Category: Woldeyes RA]]
[[Category: Van den Bedem H]]