4a2s: Difference between revisions
No edit summary |
No edit summary |
||
| (2 intermediate revisions by the same user not shown) | |||
| Line 3: | Line 3: | ||
<StructureSection load='4a2s' size='340' side='right'caption='[[4a2s]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='4a2s' size='340' side='right'caption='[[4a2s]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a2s]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a2s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A2S FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3NK:1-(6-METHOXYNAPHTHALEN-2-YL)BUTANE-1,3-DIONE'>3NK</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=4a2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a2s OCA], [https://pdbe.org/4a2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a2s RCSB], [https://www.ebi.ac.uk/pdbsum/4a2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a2s ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRPC_SACS2 TRPC_SACS2] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[ | *[[Aldolase 3D structures|Aldolase 3D structures]] | ||
*[[IGPS 3D structures|IGPS 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Saccharolobus solfataricus]] | ||
[[Category: Baker | [[Category: Baker D]] | ||
[[Category: Ban | [[Category: Ban N]] | ||
[[Category: Caner | [[Category: Caner S]] | ||
[[Category: Giger | [[Category: Giger L]] | ||
[[Category: Hilvert | [[Category: Hilvert D]] | ||
[[Category: Kast | [[Category: Kast P]] | ||
Latest revision as of 14:18, 20 December 2023
Structure of the engineered retro-aldolase RA95.5Structure of the engineered retro-aldolase RA95.5
Structural highlights
FunctionPublication Abstract from PubMedEvolutionary advances are often fueled by unanticipated innovation. Directed evolution of a computationally designed enzyme suggests that pronounced molecular changes can also drive the optimization of primitive protein active sites. The specific activity of an artificial retro-aldolase was boosted >4,400-fold by random mutagenesis and screening, affording catalytic efficiencies approaching those of natural enzymes. However, structural and mechanistic studies reveal that the engineered catalytic apparatus, consisting of a reactive lysine and an ordered water molecule, was unexpectedly abandoned in favor of a new lysine residue in a substrate-binding pocket created during the optimization process. Structures of the initial in silico design, a mechanistically promiscuous intermediate and one of the most evolved variants highlight the importance of loop mobility and supporting functional groups in the emergence of the new catalytic center. Such internal competition between alternative reactive sites may have characterized the early evolution of many natural enzymes. Evolution of a designed retro-aldolase leads to complete active site remodeling.,Giger L, Caner S, Obexer R, Kast P, Baker D, Ban N, Hilvert D Nat Chem Biol. 2013 Jun 9. doi: 10.1038/nchembio.1276. PMID:23748672[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||