3fcz

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{{Seed}}
 
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[[Image:3fcz.png|left|200px]]
 
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==Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility==
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The line below this paragraph, containing "STRUCTURE_3fcz", creates the "Structure Box" on the page.
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<StructureSection load='3fcz' size='340' side='right'caption='[[3fcz]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3fcz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FCZ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.804&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_3fcz| PDB=3fcz | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fcz OCA], [https://pdbe.org/3fcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fcz RCSB], [https://www.ebi.ac.uk/pdbsum/3fcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fcz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE] Can hydrolyze carbapenem compounds.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fc/3fcz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3fcz ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein evolution is crucial for organismal adaptation and fitness. This process takes place by shaping a given 3-dimensional fold for its particular biochemical function within the metabolic requirements and constraints of the environment. The complex interplay between sequence, structure, functionality, and stability that gives rise to a particular phenotype has limited the identification of traits acquired through evolution. This is further complicated by the fact that mutations are pleiotropic, and interactions between mutations are not always understood. Antibiotic resistance mediated by beta-lactamases represents an evolutionary paradigm in which organismal fitness depends on the catalytic efficiency of a single enzyme. Based on this, we have dissected the structural and mechanistic features acquired by an optimized metallo-beta-lactamase (MbetaL) obtained by directed evolution. We show that antibiotic resistance mediated by this enzyme is driven by 2 mutations with sign epistasis. One mutation stabilizes a catalytically relevant intermediate by fine tuning the position of 1 metal ion; whereas the other acts by augmenting the protein flexibility. We found that enzyme evolution (and the associated antibiotic resistance) occurred at the expense of the protein stability, revealing that MbetaLs have not exhausted their stability threshold. Our results demonstrate that flexibility is an essential trait that can be acquired during evolution on stable protein scaffolds. Directed evolution aided by a thorough characterization of the selected proteins can be successfully used to predict future evolutionary events and design inhibitors with an evolutionary perspective.
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===Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility===
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Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility.,Tomatis PE, Fabiane SM, Simona F, Carloni P, Sutton BJ, Vila AJ Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):20605-10. Epub 2008 Dec 19. PMID:19098096<ref>PMID:19098096</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3fcz" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_19098096}}, adds the Publication Abstract to the page
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 19098096 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_19098096}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3FCZ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FCZ OCA].
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==Reference==
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Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility., Tomatis PE, Fabiane SM, Simona F, Carloni P, Sutton BJ, Vila AJ, Proc Natl Acad Sci U S A. 2008 Dec 30;105(52):20605-10. Epub 2008 Dec 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19098096 19098096]
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[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
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[[Category: Beta-lactamase]]
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[[Category: Large Structures]]
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[[Category: Carloni, P.]]
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[[Category: Carloni P]]
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[[Category: Fabiane, S.]]
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[[Category: Fabiane S]]
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[[Category: Simona, F.]]
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[[Category: Simona F]]
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[[Category: Sutton, B.]]
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[[Category: Sutton B]]
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[[Category: Tomatis, P.]]
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[[Category: Tomatis P]]
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[[Category: Vila, A.]]
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[[Category: Vila A]]
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[[Category: Antibiotic resistance]]
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[[Category: Hydrolase]]
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[[Category: Metal-binding]]
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[[Category: Metallo-beta-lactamase]]
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[[Category: Zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 7 08:39:27 2009''
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Current revision

Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility

PDB ID 3fcz

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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