1axk
From Proteopedia
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|PDB= 1axk |SIZE=350|CAPTION= <scene name='initialview01'>1axk</scene>, resolution 2.1Å | |PDB= 1axk |SIZE=350|CAPTION= <scene name='initialview01'>1axk</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1axk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axk OCA], [http://www.ebi.ac.uk/pdbsum/1axk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1axk RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Ay, J.]] | [[Category: Ay, J.]] | ||
[[Category: Heinemann, U.]] | [[Category: Heinemann, U.]] | ||
| - | + | [[Category: 1,3-1,4-beta-glucanase]] | |
| - | [[Category: 1 | + | [[Category: 1,4-beta-xylanase]] |
| - | + | ||
| - | + | ||
| - | [[Category: 4-beta-xylanase]] | + | |
[[Category: bifunctional]] | [[Category: bifunctional]] | ||
[[Category: fusion protein]] | [[Category: fusion protein]] | ||
| Line 34: | Line 34: | ||
[[Category: hybrid enzyme]] | [[Category: hybrid enzyme]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:49:31 2008'' |
Revision as of 15:49, 30 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1
Overview
The 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.
About this Structure
1AXK is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
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
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