From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1axk.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1axk.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1axk| PDB=1axk | SCENE= }} | | {{STRUCTURE_1axk| PDB=1axk | SCENE= }} |
| | | | |
| - | '''ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_9618460}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9618460 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_9618460}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Gluxyn-1]] | | [[Category: Gluxyn-1]] |
| | [[Category: Hybrid enzyme]] | | [[Category: Hybrid enzyme]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:48:48 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 17:48:37 2008'' |
Revision as of 14:48, 30 June 2008
Template:STRUCTURE 1axk
ENGINEERED BACILLUS BIFUNCTIONAL ENZYME GLUXYN-1
Template:ABSTRACT PUBMED 9618460
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
Page seeded by OCA on Mon Jun 30 17:48:37 2008
