2mhv: Difference between revisions
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==Solution Structure of Penicillium Antifungal Protein PAF== | ==Solution Structure of Penicillium Antifungal Protein PAF== | ||
<StructureSection load='2mhv' size='340' side='right' caption='[[2mhv | <StructureSection load='2mhv' size='340' side='right'caption='[[2mhv]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mhv]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MHV OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[2mhv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Penicillium_chrysogenum Penicillium chrysogenum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MHV FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2mhv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhv OCA], [https://pdbe.org/2mhv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mhv RCSB], [https://www.ebi.ac.uk/pdbsum/2mhv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mhv ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q01701_PENCH Q01701_PENCH] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 2mhv" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Penicillium chrysogenum]] | ||
[[Category: | [[Category: Batta G]] | ||
[[Category: | [[Category: Fizil A]] | ||
Latest revision as of 11:19, 30 October 2024
Solution Structure of Penicillium Antifungal Protein PAFSolution Structure of Penicillium Antifungal Protein PAF
Structural highlights
FunctionPublication Abstract from PubMedTransition between conformational states in proteins is being recognized as a possible key factor of function. In support of this, hidden dynamic NMR structures were detected in several cases up to populations of a few percent. Here, we show by two- and three-state analysis of thermal unfolding, that the population of hidden states may weight 20-40 % at 298 K in a disulfide-rich protein. In addition, sensitive 15 N-CEST NMR experiments identified a low populated (0.15 %) state that was in slow exchange with the folded PAF protein. Remarkably, other techniques failed to identify the rest of the NMR "dark matter". Comparison of the temperature dependence of chemical shifts from experiments and molecular dynamics calculations suggests that hidden conformers of PAF differ in the loop and terminal regions and are most similar in the evolutionary conserved core. Our observations point to the existence of a complex conformational landscape with multiple conformational states in dynamic equilibrium, with diverse exchange rates presumably responsible for the completely hidden nature of a considerable fraction. "Invisible" Conformers of an Antifungal Disulfide Protein Revealed by Constrained Cold and Heat Unfolding, CEST-NMR Experiments, and Molecular Dynamics Calculations.,Fizil A, Gaspari Z, Barna T, Marx F, Batta G Chemistry. 2015 Feb 12. doi: 10.1002/chem.201404879. PMID:25676351[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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