6y2k: Difference between revisions
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The | ==Crystal structure of beta-galactosidase from the psychrophilic Marinomonas ef1== | ||
<StructureSection load='6y2k' size='340' side='right'caption='[[6y2k]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6y2k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinomonas_sp._ef1 Marinomonas sp. ef1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y2K 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]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6y2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y2k OCA], [https://pdbe.org/6y2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y2k RCSB], [https://www.ebi.ac.uk/pdbsum/6y2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y2k ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To survive in cold environments, psychrophilic organisms produce enzymes endowed with high specific activity at low temperature. The structure of these enzymes is usually flexible and mostly thermolabile. In this work, we investigate the structural basis of cold adaptation of a GH42 beta-galactosidase from the psychrophilic Marinomonas ef1. This enzyme couples cold activity with astonishing robustness for a psychrophilic protein, for it retains 23% of its highest activity at 5 degrees C and it is stable for several days at 37 degrees C and even 50 degrees C. Phylogenetic analyses indicate a close relationship with thermophilic beta-galactosidases, suggesting that the present-day enzyme evolved from a thermostable scaffold modeled by environmental selective pressure. The crystallographic structure reveals the overall similarity with GH42 enzymes, along with a hexameric arrangement (dimer of trimers) not found in psychrophilic, mesophilic and thermophilic homologues. In the quaternary structure, protomers form a large central cavity, whose accessibility to the substrate is promoted by the dynamic behavior of surface loops, even at low temperature. This peculiar temperature-driven cooperative behavior of the enzyme is likely related to the increase of the internal cavity permeability triggered by heating. Overall, our results highlight a novel strategy of enzyme cold adaptation, based on the oligomerization state of the enzyme, which effectively challenges the paradigm of cold activity coupled with intrinsic thermolability. | |||
The co-existence of cold activity and thermal stability in an Antarctic GH42 beta-galactosidase relies on its hexametric quaternary arrangement.,Mangiagalli M, Lapi M, Maione S, Orlando M, Brocca S, Pesce A, Barbiroli A, Camilloni C, Pucciarelli S, Lotti M, Nardini M FEBS J. 2020 May 4. doi: 10.1111/febs.15354. PMID:32363751<ref>PMID:32363751</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6y2k" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Galactosidase 3D structures|Galactosidase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Marinomonas sp. ef1]] | ||
[[Category: Barbiroli A]] | |||
[[Category: Brocca S]] | |||
[[Category: Camilloni C]] | |||
[[Category: Lapi M]] | |||
[[Category: Lotti M]] | |||
[[Category: Maione S]] | |||
[[Category: Mangiagalli M]] | |||
[[Category: Orlando M]] | |||
[[Category: Pesce A]] | |||
[[Category: Pucciarelli S]] | |||
Latest revision as of 16:18, 24 January 2024
Crystal structure of beta-galactosidase from the psychrophilic Marinomonas ef1Crystal structure of beta-galactosidase from the psychrophilic Marinomonas ef1
Structural highlights
Publication Abstract from PubMedTo survive in cold environments, psychrophilic organisms produce enzymes endowed with high specific activity at low temperature. The structure of these enzymes is usually flexible and mostly thermolabile. In this work, we investigate the structural basis of cold adaptation of a GH42 beta-galactosidase from the psychrophilic Marinomonas ef1. This enzyme couples cold activity with astonishing robustness for a psychrophilic protein, for it retains 23% of its highest activity at 5 degrees C and it is stable for several days at 37 degrees C and even 50 degrees C. Phylogenetic analyses indicate a close relationship with thermophilic beta-galactosidases, suggesting that the present-day enzyme evolved from a thermostable scaffold modeled by environmental selective pressure. The crystallographic structure reveals the overall similarity with GH42 enzymes, along with a hexameric arrangement (dimer of trimers) not found in psychrophilic, mesophilic and thermophilic homologues. In the quaternary structure, protomers form a large central cavity, whose accessibility to the substrate is promoted by the dynamic behavior of surface loops, even at low temperature. This peculiar temperature-driven cooperative behavior of the enzyme is likely related to the increase of the internal cavity permeability triggered by heating. Overall, our results highlight a novel strategy of enzyme cold adaptation, based on the oligomerization state of the enzyme, which effectively challenges the paradigm of cold activity coupled with intrinsic thermolability. The co-existence of cold activity and thermal stability in an Antarctic GH42 beta-galactosidase relies on its hexametric quaternary arrangement.,Mangiagalli M, Lapi M, Maione S, Orlando M, Brocca S, Pesce A, Barbiroli A, Camilloni C, Pucciarelli S, Lotti M, Nardini M FEBS J. 2020 May 4. doi: 10.1111/febs.15354. PMID:32363751[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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