|
|
| (3 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==Chimeric Family 1 beta-glucosidase made with non-contiguous SCHEMA== | | ==Chimeric Family 1 beta-glucosidase made with non-contiguous SCHEMA== |
| - | <StructureSection load='4gxp' size='340' side='right' caption='[[4gxp]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='4gxp' size='340' side='right'caption='[[4gxp]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gxp]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GXP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gxp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8] and [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GXP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wbg|2wbg]], [[3ahy|3ahy]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bglA, bgl2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=51453 ATCC 13631])</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=4gxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxp OCA], [https://pdbe.org/4gxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gxp RCSB], [https://www.ebi.ac.uk/pdbsum/4gxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxp ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-glucosidase Beta-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.21 3.2.1.21] </span></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=4gxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gxp RCSB], [http://www.ebi.ac.uk/pdbsum/4gxp PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/BGLA_THEMA BGLA_THEMA] [https://www.uniprot.org/uniprot/O93785_HYPJE O93785_HYPJE] |
| - | We introduce a method for identifying elements of a protein structure that can be shuffled to make chimeric proteins from two or more homologous parents. Formulating recombination as a graph-partitioning problem allows us to identify noncontiguous segments of the sequence that should be inherited together in the progeny proteins. We demonstrate this noncontiguous recombination approach by constructing a chimera of beta-glucosidases from two different kingdoms of life. Although the protein's alpha-beta barrel fold has no obvious subdomains for recombination, noncontiguous SCHEMA recombination generated a functional chimera that takes approximately half its structure from each parent. The X-ray crystal structure shows that the structural blocks that make up the chimera maintain the backbone conformations found in their respective parental structures. Although the chimera has lower beta-glucosidase activity than the parent enzymes, the activity was easily recovered by directed evolution. This simple method, which does not rely on detailed atomic models, can be used to design chimeras that take structural, and functional, elements from distantly-related proteins.
| + | |
| - | | + | |
| - | Chimeragenesis of distantly-related proteins by noncontiguous recombination.,Smith MA, Romero PA, Wu T, Brustad EM, Arnold FH Protein Sci. 2012 Dec 6. doi: 10.1002/pro.2202. PMID:23225662<ref>PMID:23225662</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Beta-glucosidase|Beta-glucosidase]] | + | *[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 13631]] | + | [[Category: Large Structures]] |
| - | [[Category: Beta-glucosidase]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Arnold, F H]] | + | [[Category: Trichoderma reesei]] |
| - | [[Category: Brustad, E M]] | + | [[Category: Arnold FH]] |
| - | [[Category: Romero, P A]] | + | [[Category: Brustad EM]] |
| - | [[Category: Smith, M A]] | + | [[Category: Romero PA]] |
| - | [[Category: Wu, T]] | + | [[Category: Smith MA]] |
| - | [[Category: Chimeragenesis]] | + | [[Category: Wu T]] |
| - | [[Category: Eukaryotic-prokaryotic chimera]]
| + | |
| - | [[Category: Gh1]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protein recombination]]
| + | |
