From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1mve.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1mve.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1mve| PDB=1mve | SCENE= }} | | {{STRUCTURE_1mve| PDB=1mve | SCENE= }} |
| | | | |
| - | '''Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes'''
| + | ===Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes (Fsbeta-glucanase) is classified as one of the family 16 glycosyl hydrolases. It hydrolyzes the glycosidic bond in the mixed-linked glucans containing beta-1,3- and beta-1,4-glycosidic linkages. We constructed a truncated form of recombinant Fsbeta-glucanase containing the catalytic domain from amino acid residues 1-258, which exhibited a higher thermal stability and enzymatic activity than the full-length enzyme. The crystal structure of the truncated Fsbeta-glucanase was solved at a resolution of 1.7A by the multiple wavelength anomalous dispersion (MAD) method using the anomalous signals from the seleno-methionine-labeled protein. The overall topology of the truncated Fsbeta-glucanase consists mainly of two eight-stranded anti-parallel beta-sheets arranged in a jellyroll beta-sandwich, similar to the fold of many glycosyl hydrolases and carbohydrate-binding modules. Sequence comparison with other bacterial glucanases showed that Fsbeta-glucanase is the only naturally occurring circularly permuted beta-glucanase with reversed sequences. Structural comparison shows that the engineered circular-permuted Bacillus enzymes are more similar to their parent enzymes with which they share approximately 70% sequence identity, than to the naturally occurring Fsbeta-glucanase of similar topology with 30% identity. This result suggests that protein structure relies more on sequence identity than topology. The high-resolution structure of Fsbeta-glucanase provides a structural rationale for the different activities obtained from a series of mutant glucanases and a basis for the development of engineered enzymes with increased activity and structural stability. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12842475}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12842475 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12842475}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 29: |
Line 33: |
| | [[Category: Yuan, H S.]] | | [[Category: Yuan, H S.]] |
| | [[Category: Circular-permutated jellyroll protein]] | | [[Category: Circular-permutated jellyroll protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:45:51 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:48:41 2008'' |
Revision as of 13:48, 28 July 2008
Template:STRUCTURE 1mve
Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes
Template:ABSTRACT PUBMED 12842475
About this Structure
1MVE is a Single protein structure of sequence from Fibrobacter succinogenes. Full crystallographic information is available from OCA.
Reference
Crystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes., Tsai LC, Shyur LF, Lee SH, Lin SS, Yuan HS, J Mol Biol. 2003 Jul 11;330(3):607-20. PMID:12842475
Page seeded by OCA on Mon Jul 28 16:48:41 2008
