1axk: Difference between revisions
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<StructureSection load='1axk' size='340' side='right'caption='[[1axk]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1axk' size='340' side='right'caption='[[1axk]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1axk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AXK FirstGlance]. <br> | <table><tr><td colspan='2'>[[1axk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AXK FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 2.1Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1axk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axk OCA], [https://pdbe.org/1axk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1axk RCSB], [https://www.ebi.ac.uk/pdbsum/1axk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1axk ProSAT]</span></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=1axk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axk OCA], [https://pdbe.org/1axk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1axk RCSB], [https://www.ebi.ac.uk/pdbsum/1axk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1axk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/GUB_PAEMA GUB_PAEMA] [https://www.uniprot.org/uniprot/XYNA_BACSU XYNA_BACSU] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus subtilis]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Ay | [[Category: Ay J]] | ||
[[Category: Heinemann | [[Category: Heinemann U]] | ||
Revision as of 13:57, 2 August 2023
ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 1,3-1,4-beta-glucanase from Bacillus macerans (wtGLU) and the 1, 4-beta-xylanase from Bacillus subtilis (wtXYN) are both single-domain jellyroll proteins catalyzing similar enzymatic reactions. In the fusion protein GluXyn-1, the two proteins are joined by insertion of the entire XYN domain into a surface loop of cpMAC-57, a circularly permuted variant of wtGLU. GluXyn-1 was generated by protein engineering methods, produced in Escherichia coli and shown to fold spontaneously and have both enzymatic activities at wild-type level. The crystal structure of GluXyn-1 was determined at 2.1 A resolution and refined to R = 17.7% and R(free) = 22.4%. It shows nearly ideal, native-like folding of both protein domains and a small, but significant hinge bending between the domains. The active sites are independent and accessible explaining the observed enzymatic activity. Because in GluXyn-1 the complete XYN domain is inserted into the compact folding unit of GLU, the wild-type-like activity and tertiary structure of the latter proves that the folding process of GLU does not depend on intramolecular interactions that are short-ranged in the sequence. Insertion fusions of the GluXyn-1 type may prove to be an easy route toward more stable bifunctional proteins in which the two parts are more closely associated than in linear end-to-end protein fusions. Structure and function of the Bacillus hybrid enzyme GluXyn-1: native-like jellyroll fold preserved after insertion of autonomous globular domain.,Ay J, Gotz F, Borriss R, Heinemann U Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6613-8. PMID:9618460[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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