6lvw: Difference between revisions
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==Polyextremophilic Beta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi== | ==Polyextremophilic Beta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi== | ||
<StructureSection load='6lvw' size='340' side='right'caption='[[6lvw]]' scene=''> | <StructureSection load='6lvw' size='340' side='right'caption='[[6lvw]], [[Resolution|resolution]] 2.49Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LVW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LVW FirstGlance]. <br> | <table><tr><td colspan='2'>[[6lvw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hallt Hallt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LVW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LVW FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lvw OCA], [http://pdbe.org/6lvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lvw RCSB], [http://www.ebi.ac.uk/pdbsum/6lvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lvw ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hlac_2868 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=416348 HALLT])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-galactosidase Beta-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.23 3.2.1.23] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6lvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lvw OCA], [http://pdbe.org/6lvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lvw RCSB], [http://www.ebi.ac.uk/pdbsum/6lvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lvw ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/BGAL_HALLT BGAL_HALLT]] Cleaves o-nitrophenyl-beta-D-galactopyranoside (ONPG) in vitro.<ref>PMID:23320757</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The haloarchaeon Halorubrum lacusprofundi is among the few polyextremophilic organisms capable of surviving in one of the most extreme aquatic environments on Earth, the Deep Lake of Antarctica (-18 degrees C to +11.5 degrees C and 21-28%, w/v salt content). Hence, H. lacusprofundi has been proposed as a model for biotechnology and astrobiology to investigate potential life beyond Earth. To understand the mechanisms that allow proteins to adapt to both salinity and cold, we structurally (including X-ray crystallography and molecular dynamics simulations) and functionally characterized the beta-galactosidase from H. lacusprofundi (hla_bga). Recombinant hla_bga (produced in Haloferax volcanii) revealed exceptional stability, tolerating up to 4 M NaCl and up to 20% (v/v) of organic solvents. Despite being cold-adapted, hla_bga was also stable up to 60 degrees C. Structural analysis showed that hla_bga combined increased surface acidity (associated with halophily) with increased structural flexibility, fine-tuned on a residue level, for sustaining activity at low temperatures. The resulting blend enhanced structural flexibility at low temperatures but also limited protein movements at higher temperatures relative to mesophilic homologs. Collectively, these observations help in understanding the molecular basis of a dual psychrophilic and halophilic adaptation and suggest that such enzymes may be intrinsically stable and functional over an exceptionally large temperature range. | |||
Understanding High-Salt and Cold Adaptation of a Polyextremophilic Enzyme.,Karan R, Mathew S, Muhammad R, Bautista DB, Vogler M, Eppinger J, Oliva R, Cavallo L, Arold ST, Rueping M Microorganisms. 2020 Oct 16;8(10). pii: microorganisms8101594. doi:, 10.3390/microorganisms8101594. PMID:33081237<ref>PMID:33081237</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6lvw" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Beta-galactosidase]] | |||
[[Category: Hallt]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Arold | [[Category: Arold, S T]] | ||
[[Category: Muhammad R]] | [[Category: Muhammad, R]] | ||
[[Category: Extremophile]] | |||
[[Category: Extremozyme]] | |||
[[Category: Halophile]] | |||
[[Category: Hydrolase]] | |||
[[Category: Polyextremophilic enzyme]] | |||
[[Category: Psychrophile]] | |||
[[Category: Sugar binding protein]] | |||
Revision as of 10:31, 4 November 2020
Polyextremophilic Beta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundiPolyextremophilic Beta-galactosidase from the Antarctic haloarchaeon Halorubrum lacusprofundi
Structural highlights
Function[BGAL_HALLT] Cleaves o-nitrophenyl-beta-D-galactopyranoside (ONPG) in vitro.[1] Publication Abstract from PubMedThe haloarchaeon Halorubrum lacusprofundi is among the few polyextremophilic organisms capable of surviving in one of the most extreme aquatic environments on Earth, the Deep Lake of Antarctica (-18 degrees C to +11.5 degrees C and 21-28%, w/v salt content). Hence, H. lacusprofundi has been proposed as a model for biotechnology and astrobiology to investigate potential life beyond Earth. To understand the mechanisms that allow proteins to adapt to both salinity and cold, we structurally (including X-ray crystallography and molecular dynamics simulations) and functionally characterized the beta-galactosidase from H. lacusprofundi (hla_bga). Recombinant hla_bga (produced in Haloferax volcanii) revealed exceptional stability, tolerating up to 4 M NaCl and up to 20% (v/v) of organic solvents. Despite being cold-adapted, hla_bga was also stable up to 60 degrees C. Structural analysis showed that hla_bga combined increased surface acidity (associated with halophily) with increased structural flexibility, fine-tuned on a residue level, for sustaining activity at low temperatures. The resulting blend enhanced structural flexibility at low temperatures but also limited protein movements at higher temperatures relative to mesophilic homologs. Collectively, these observations help in understanding the molecular basis of a dual psychrophilic and halophilic adaptation and suggest that such enzymes may be intrinsically stable and functional over an exceptionally large temperature range. Understanding High-Salt and Cold Adaptation of a Polyextremophilic Enzyme.,Karan R, Mathew S, Muhammad R, Bautista DB, Vogler M, Eppinger J, Oliva R, Cavallo L, Arold ST, Rueping M Microorganisms. 2020 Oct 16;8(10). pii: microorganisms8101594. doi:, 10.3390/microorganisms8101594. PMID:33081237[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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