5tuj: Difference between revisions

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==Ancestral Cationic Amino Acid Solute Binding Protein (AncCDT-1)==
==Ancestral Cationic Amino Acid Solute Binding Protein (AncCDT-1)==
<StructureSection load='5tuj' size='340' side='right' caption='[[5tuj]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
<StructureSection load='5tuj' size='340' side='right'caption='[[5tuj]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5tuj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TUJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[5tuj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Miscellaneous_nucleic_acid Miscellaneous nucleic acid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TUJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5TUJ FirstGlance]. <br>
</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=5tuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tuj OCA], [http://pdbe.org/5tuj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tuj RCSB], [http://www.ebi.ac.uk/pdbsum/5tuj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tuj ProSAT]</span></td></tr>
</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=5tuj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tuj OCA], [http://pdbe.org/5tuj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tuj RCSB], [http://www.ebi.ac.uk/pdbsum/5tuj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tuj ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Miscellaneous nucleic acid]]
[[Category: Miscellaneous nucleic acid]]
[[Category: Carr, P D]]
[[Category: Carr, P D]]

Revision as of 12:09, 21 October 2020

Ancestral Cationic Amino Acid Solute Binding Protein (AncCDT-1)Ancestral Cationic Amino Acid Solute Binding Protein (AncCDT-1)

Structural highlights

5tuj is a 1 chain structure with sequence from Miscellaneous nucleic acid. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

The emergence of enzymes through the neofunctionalization of noncatalytic proteins is ultimately responsible for the extraordinary range of biological catalysts observed in nature. Although the evolution of some enzymes from binding proteins can be inferred by homology, we have a limited understanding of the nature of the biochemical and biophysical adaptations along these evolutionary trajectories and the sequence in which they occurred. Here we reconstructed and characterized evolutionary intermediate states linking an ancestral solute-binding protein to the extant enzyme cyclohexadienyl dehydratase. We show how the intrinsic reactivity of a desolvated general acid was harnessed by a series of mutations radiating from the active site, which optimized enzyme-substrate complementarity and transition-state stabilization and minimized sampling of noncatalytic conformations. Our work reveals the molecular evolutionary processes that underlie the emergence of enzymes de novo, which are notably mirrored by recent examples of computational enzyme design and directed evolution.

Evolution of cyclohexadienyl dehydratase from an ancestral solute-binding protein.,Clifton BE, Kaczmarski JA, Carr PD, Gerth ML, Tokuriki N, Jackson CJ Nat Chem Biol. 2018 Apr 23. pii: 10.1038/s41589-018-0043-2. doi:, 10.1038/s41589-018-0043-2. PMID:29686357[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Clifton BE, Kaczmarski JA, Carr PD, Gerth ML, Tokuriki N, Jackson CJ. Evolution of cyclohexadienyl dehydratase from an ancestral solute-binding protein. Nat Chem Biol. 2018 Apr 23. pii: 10.1038/s41589-018-0043-2. doi:, 10.1038/s41589-018-0043-2. PMID:29686357 doi:http://dx.doi.org/10.1038/s41589-018-0043-2

5tuj, resolution 3.35Å

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OCA