6bm9: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6bm9 is ON HOLD
+==Directed evolutionary changes in MBL super family - VIM-2 Round 10==
+<StructureSection load='6bm9' size='340' side='right'caption='[[6bm9]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6bm9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BM9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BM9 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]] 2.19&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6bm9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bm9 OCA], [https://pdbe.org/6bm9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bm9 RCSB], [https://www.ebi.ac.uk/pdbsum/6bm9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bm9 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q5U7L7_ECOLX Q5U7L7_ECOLX]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Genetic variation among orthologous proteins can cause cryptic phenotypic properties that only manifest in changing environments. Such variation may impact the evolvability of proteins, but the underlying molecular basis remains unclear. Here, we performed comparative directed evolution of four orthologous metallo-beta-lactamases toward a new function and found that different starting genotypes evolved to distinct evolutionary outcomes. Despite a low initial fitness, one ortholog reached a significantly higher fitness plateau than its counterparts, via increasing catalytic activity. By contrast, the ortholog with the highest initial activity evolved to a less-optimal and phenotypically distinct outcome through changes in expression, oligomerization and activity. We show how cryptic molecular properties and conformational variation of active site residues in the initial genotypes cause epistasis, that could lead to distinct evolutionary outcomes. Our work highlights the importance of understanding the molecular details that connect genetic variation to protein function to improve the prediction of protein evolution.
-Authors: Hong, N.-S., Jackson, C.J., Carr, P.D.
+Cryptic genetic variation shapes the adaptive evolutionary potential of enzymes.,Baier F, Hong N, Yang G, Pabis A, Miton CM, Barrozo A, Carr PD, Kamerlin SC, Jackson CJ, Tokuriki N Elife. 2019 Feb 5;8. pii: 40789. doi: 10.7554/eLife.40789. PMID:30719972<ref>PMID:30719972</ref>
-Description: Directed evolutionary changes in MBL super family -VIM-2 Round 10
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Hong, N.-S]]
+<div class="pdbe-citations 6bm9" style="background-color:#fffaf0;"></div>
-[[Category: Jackson, C.J]]
-[[Category: Carr, P.D]]
+==See Also==
+*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
+[[Category: Carr PD]]
+[[Category: Hong N-S]]
+[[Category: Jackson CJ]]