6ggp: Difference between revisions
New page: '''Unreleased structure''' The entry 6ggp is ON HOLD Authors: Smaldone, G., Berisio, R., Balasco, N., D'Auria, S., Vitagliano, L., Ruggiero, A. Description: Structure of the apo form o... |
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The | ==Structure of the ligand-free form of truncated ArgBP (residues 20-233) from T. maritima== | ||
<StructureSection load='6ggp' size='340' side='right' caption='[[6ggp]], [[Resolution|resolution]] 1.03Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ggp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GGP FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_0593 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ggp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ggp OCA], [http://pdbe.org/6ggp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ggp RCSB], [http://www.ebi.ac.uk/pdbsum/6ggp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ggp ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Thermotoga maritima Arginine Binding Protein (TmArgBP) is a valuable candidate for arginine biosensing in diagnostics. This protein is endowed with unusual structural properties that include an extraordinary thermal/chemical stability, a domain swapped structure that undergoes large tertiary and quaternary structural transition, and the ability to form non-canonical oligomeric species. As the intrinsic stability of TmArgBP allows for extensive protein manipulations, we here dissected its structure in two parts: its main body deprived of the swapping fragment (TmArgBP(20-233)) and the C-terminal peptide corresponding to the helical swapping element. Both elements have been characterized independently or in combination using a repertoire of biophysical/structural techniques. Present investigations clearly indicate that TmArgBP(20-233) represents a better scaffold for arginine sensing compared to the wild-type protein. Moreover, our data demonstrate that the ligand-free and the ligand-bound forms respond very differently to this helix deletion. This drastic perturbation has an important impact on the ligand-bound form of TmArgBP(20-233) stability whereas it barely affects its ligand-free state. The crystallographic structures of these forms provide a rationale to this puzzling observation. Indeed, the arginine-bound state is very rigid and virtually unchanged upon protein truncation. On the other hand, the flexible ligand-free TmArgBP(20-233) is able to adopt a novel state as a consequence of the helix deletion. Therefore, the flexibility of the ligand-free form endows this state with a remarkable robustness upon severe perturbations. In this scenario, TmArgBP dissection highlights an intriguing connection between destabilizing/stabilizing effects and the overall flexibility that could operate also in other proteins. | |||
Domain swapping dissection in Thermotoga maritima arginine binding protein: How structural flexibility may compensate destabilization.,Smaldone G, Berisio R, Balasco N, D'Auria S, Vitagliano L, Ruggiero A Biochim Biophys Acta. 2018 May 31;1866(9):952-962. doi:, 10.1016/j.bbapap.2018.05.016. PMID:29860047<ref>PMID:29860047</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6ggp" style="background-color:#fffaf0;"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Thema]] | |||
[[Category: Auria, S D]] | |||
[[Category: Balasco, N]] | [[Category: Balasco, N]] | ||
[[Category: Berisio, R]] | |||
[[Category: Ruggiero, A]] | |||
[[Category: Smaldone, G]] | [[Category: Smaldone, G]] | ||
[[Category: Vitagliano, L]] | [[Category: Vitagliano, L]] | ||
[[Category: | [[Category: Argininemia diagnosis]] | ||
[[Category: Biosensor]] | |||
[[Category: Calorimetry]] | |||
[[Category: Domain swapping]] | |||
[[Category: Protein structure-stability]] | |||
[[Category: Transport protein]] | |||
Latest revision as of 09:35, 20 June 2018
Structure of the ligand-free form of truncated ArgBP (residues 20-233) from T. maritimaStructure of the ligand-free form of truncated ArgBP (residues 20-233) from T. maritima
Structural highlights
Publication Abstract from PubMedThermotoga maritima Arginine Binding Protein (TmArgBP) is a valuable candidate for arginine biosensing in diagnostics. This protein is endowed with unusual structural properties that include an extraordinary thermal/chemical stability, a domain swapped structure that undergoes large tertiary and quaternary structural transition, and the ability to form non-canonical oligomeric species. As the intrinsic stability of TmArgBP allows for extensive protein manipulations, we here dissected its structure in two parts: its main body deprived of the swapping fragment (TmArgBP(20-233)) and the C-terminal peptide corresponding to the helical swapping element. Both elements have been characterized independently or in combination using a repertoire of biophysical/structural techniques. Present investigations clearly indicate that TmArgBP(20-233) represents a better scaffold for arginine sensing compared to the wild-type protein. Moreover, our data demonstrate that the ligand-free and the ligand-bound forms respond very differently to this helix deletion. This drastic perturbation has an important impact on the ligand-bound form of TmArgBP(20-233) stability whereas it barely affects its ligand-free state. The crystallographic structures of these forms provide a rationale to this puzzling observation. Indeed, the arginine-bound state is very rigid and virtually unchanged upon protein truncation. On the other hand, the flexible ligand-free TmArgBP(20-233) is able to adopt a novel state as a consequence of the helix deletion. Therefore, the flexibility of the ligand-free form endows this state with a remarkable robustness upon severe perturbations. In this scenario, TmArgBP dissection highlights an intriguing connection between destabilizing/stabilizing effects and the overall flexibility that could operate also in other proteins. Domain swapping dissection in Thermotoga maritima arginine binding protein: How structural flexibility may compensate destabilization.,Smaldone G, Berisio R, Balasco N, D'Auria S, Vitagliano L, Ruggiero A Biochim Biophys Acta. 2018 May 31;1866(9):952-962. doi:, 10.1016/j.bbapap.2018.05.016. PMID:29860047[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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