1axk: Difference between revisions
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[[Image:1axk.gif|left|200px]] | [[Image:1axk.gif|left|200px]] | ||
'''ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1''' | {{Structure | ||
|PDB= 1axk |SIZE=350|CAPTION= <scene name='initialview01'>1axk</scene>, resolution 2.1Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AXK is a [ | 1AXK is a [[Single protein]] structure of sequence from [http://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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9618460 9618460] | ||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: hybrid enzyme]] | [[Category: hybrid enzyme]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:03:30 2008'' | ||
Revision as of 11:03, 20 March 2008
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ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1
OverviewOverview
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 StructureAbout this Structure
1AXK is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
ReferenceReference
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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