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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mvz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_kaustophilus_HTA426 Geobacillus kaustophilus HTA426]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MVZ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mvz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_kaustophilus_HTA426 Geobacillus kaustophilus HTA426]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MVZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MVZ 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=2mvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mvz OCA], [https://pdbe.org/2mvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mvz RCSB], [https://www.ebi.ac.uk/pdbsum/2mvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mvz 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=2mvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mvz OCA], [https://pdbe.org/2mvz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mvz RCSB], [https://www.ebi.ac.uk/pdbsum/2mvz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mvz ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/Q5KXK3_GEOKA Q5KXK3_GEOKA] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]
[https://www.uniprot.org/uniprot/Q5KXK3_GEOKA Q5KXK3_GEOKA] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Thermophilic proteins have found extensive use in research and industrial applications because of their high stability and functionality at elevated temperatures while simultaneously providing valuable insight into our understanding of protein folding, stability, dynamics, and function. Cyclophilins, constituting a ubiquitously expressed family of peptidyl-prolyl isomerases with a range of biological functions and disease associations, have been utilized both for conferring stress tolerances and in exploring the link between conformational dynamics and enzymatic function. To date, however, no active thermophilic cyclophilin has been fully biophysically characterized. Here, we determine the structure of a thermophilic cyclophilin (GeoCyp) from Geobacillus kaustophilus, characterize its dynamic motions over several time scales using an array of methodologies that include chemical shift-based methods and relaxation experiments over a range of temperatures, and measure catalytic activity over a range of temperatures to compare its structure, dynamics, and function to those of a mesophilic counterpart, human cyclophilin A (CypA). Unlike those of most thermophile/mesophile pairs, GeoCyp catalysis is not substantially impaired at low temperatures as compared to that of CypA, retaining approximately 70% of the activity of its mesophilic counterpart. Examination of substrate-bound ensembles reveals a mechanism by which the two cyclophilins may have adapted to their environments through altering dynamic loop motions and a critical residue that acts as a clamp to regulate substrate binding differentially in CypA and GeoCyp. Fast time scale (pico- to nanosecond) dynamics are largely conserved between the two proteins, in accordance with the high degree of structural similarity, although differences do exist in their temperature dependencies. Slower (microsecond) time scale motions are likewise localized to similar regions in the two proteins with some variability in their magnitudes yet do not exhibit significant temperature dependencies in either enzyme.
Structure and Dynamics of GeoCyp: A Thermophilic Cyclophilin with a Novel Substrate Binding Mechanism That Functions Efficiently at Low Temperatures.,Holliday MJ, Camilloni C, Armstrong GS, Isern NG, Zhang F, Vendruscolo M, Eisenmesser EZ Biochemistry. 2015 May 26;54(20):3207-17. doi: 10.1021/acs.biochem.5b00263. Epub , 2015 May 14. PMID:25923019<ref>PMID:25923019</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mvz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
</StructureSection>

Latest revision as of 07:02, 1 May 2024

Solution Structure for Cyclophilin A from Geobacillus Kaustophilus

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