5c9y: Difference between revisions
No edit summary |
No edit summary |
||
| (4 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crystal structure of yellow lupine LlPR-10.1A protein partially saturated with trans-zeatin== | |||
<StructureSection load='5c9y' size='340' side='right'caption='[[5c9y]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5c9y]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lupinus_luteus Lupinus luteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C9Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C9Y 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]] 1.5Å</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=5c9y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c9y OCA], [https://pdbe.org/5c9y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c9y RCSB], [https://www.ebi.ac.uk/pdbsum/5c9y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c9y ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/L18A_LUPLU L18A_LUPLU] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Plant pathogenesis-related class 10 (PR-10) proteins are a family of abundant proteins initially identified as elements of the plant defense system. The key structural feature suggesting PR-10 functionality is a huge hydrophobic cavity created in the protein interior by a scaffold composed of an extended beta-sheet wrapped around a long and flexible C-terminal alpha-helix. Several crystallographic and NMR studies have shown that the cavity can accommodate a variety of small molecule ligands, including phytohormones. The article describes approximately 1.3A resolution crystal structures of a Lupinus luteus PR-10 isoform LlPR-10.1A, in its free form and in complex with trans-zeatin, a naturally occurring plant hormone belonging to the cytokinin group. Moreover we present the structure of the same protein where the saturation with zeatin is not complete. This set of three crystal structures allows us to track the structural adaptation of the protein upon trans-zeatin docking, as well as the sequence of the ligand-binding events, step-by-step. In addition, titration of LlPR-10.1A with trans-zeatin monitored in solution by CD spectra, confirmed the pattern of structural adaptations deduced from the crystallographic studies. The ligand-biding mode shows no similarity to other zeatin complexes of PR-10 proteins. The present work, which describes the first atomic models of the same PR-10 protein with and without a physiological ligand, reveals that the conformation of LlPR-10.1A undergoes a significant structural rearrangement upon trans-zeatin binding. | |||
Crystallographic and CD probing of ligand-induced conformational changes in a plant PR-10 protein.,Sliwiak J, Dolot R, Michalska K, Szpotkowski K, Bujacz G, Sikorski M, Jaskolski M J Struct Biol. 2015 Nov 28. pii: S1047-8477(15)30105-2. doi:, 10.1016/j.jsb.2015.11.008. PMID:26644353<ref>PMID:26644353</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5c9y" style="background-color:#fffaf0;"></div> | ||
[[Category: Sikorski | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Lupinus luteus]] | |||
[[Category: Jaskolski M]] | |||
[[Category: Sikorski MM]] | |||
[[Category: Sliwiak J]] | |||
Latest revision as of 14:19, 10 January 2024
Crystal structure of yellow lupine LlPR-10.1A protein partially saturated with trans-zeatinCrystal structure of yellow lupine LlPR-10.1A protein partially saturated with trans-zeatin
Structural highlights
FunctionPublication Abstract from PubMedPlant pathogenesis-related class 10 (PR-10) proteins are a family of abundant proteins initially identified as elements of the plant defense system. The key structural feature suggesting PR-10 functionality is a huge hydrophobic cavity created in the protein interior by a scaffold composed of an extended beta-sheet wrapped around a long and flexible C-terminal alpha-helix. Several crystallographic and NMR studies have shown that the cavity can accommodate a variety of small molecule ligands, including phytohormones. The article describes approximately 1.3A resolution crystal structures of a Lupinus luteus PR-10 isoform LlPR-10.1A, in its free form and in complex with trans-zeatin, a naturally occurring plant hormone belonging to the cytokinin group. Moreover we present the structure of the same protein where the saturation with zeatin is not complete. This set of three crystal structures allows us to track the structural adaptation of the protein upon trans-zeatin docking, as well as the sequence of the ligand-binding events, step-by-step. In addition, titration of LlPR-10.1A with trans-zeatin monitored in solution by CD spectra, confirmed the pattern of structural adaptations deduced from the crystallographic studies. The ligand-biding mode shows no similarity to other zeatin complexes of PR-10 proteins. The present work, which describes the first atomic models of the same PR-10 protein with and without a physiological ligand, reveals that the conformation of LlPR-10.1A undergoes a significant structural rearrangement upon trans-zeatin binding. Crystallographic and CD probing of ligand-induced conformational changes in a plant PR-10 protein.,Sliwiak J, Dolot R, Michalska K, Szpotkowski K, Bujacz G, Sikorski M, Jaskolski M J Struct Biol. 2015 Nov 28. pii: S1047-8477(15)30105-2. doi:, 10.1016/j.jsb.2015.11.008. PMID:26644353[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||