9rbp: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Structure of an ancestral bifunctional dehalogenase-luciferase enzyme Anc238Loc, space group P21212== | |||
<StructureSection load='9rbp' size='340' side='right'caption='[[9rbp]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9rbp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RBP 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]] 2.199Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=9rbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9rbp OCA], [https://pdbe.org/9rbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9rbp RCSB], [https://www.ebi.ac.uk/pdbsum/9rbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9rbp ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The alpha/beta-hydrolase (ABH) superfamily is a widespread and functionally versatile protein fold recognized for its ability to adapt to diverse molecular functions across all three domains of life. One such spectacular example of evolutionary adaptation at the ABH fold is an acquisition of oxygenolytic luciferase reaction that occurred within the hydrolytic haloalkane dehalogenase family. The molecular details of this evolution remain puzzling. In this work, we determine crystal structures and explore dynamical behaviour of a bifunctional ancestral ABH-fold enzyme, highlighting molecular features associated with the transition from hydrolytic to oxygenolytic catalysis at this fold. Structures showed a canonical alphabetaalpha-sandwich shielded with a helical cap domain. The catalytic pocket is voluminous enough to accommodate a bulky substrate. Molecular dynamics simulations demonstrated that coelenterazine entry does not present a major energetic barrier and identified a preferred binding orientation important for oxygenolytic catalysis. Comparisons between ancestral and extant enzymes highlighted specific amino acids and sequence motifs characteristic for oxygenolytic luciferases. Collectively, our results provide an expanded view of the evolutionary transition in which ABH-fold enzymes, originally using water to cleave chemical bonds, adapted to utilize dioxygen for bioluminescence. | |||
Structural insights into the evolution of alpha/beta-hydrolase fold luciferases.,Majerova M, Horackova J, Sedlackova K, Sulova M, Kovar D, Damborsky J, Prokop Z, Bednar D, Marek M Int J Biol Macromol. 2026 May;361:151870. doi: 10.1016/j.ijbiomac.2026.151870. , Epub 2026 Apr 6. PMID:41951082<ref>PMID:41951082</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9rbp" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synthetic construct]] | |||
[[Category: Majerova M]] | |||
[[Category: Marek M]] | |||
Latest revision as of 04:58, 27 May 2026
Structure of an ancestral bifunctional dehalogenase-luciferase enzyme Anc238Loc, space group P21212
| ||||||||||||
