1mve
From Proteopedia
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|PDB= 1mve |SIZE=350|CAPTION= <scene name='initialview01'>1mve</scene>, resolution 1.70Å | |PDB= 1mve |SIZE=350|CAPTION= <scene name='initialview01'>1mve</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Licheninase Licheninase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.73 3.2.1.73] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mve FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mve OCA], [http://www.ebi.ac.uk/pdbsum/1mve PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mve RCSB]</span> | ||
}} | }} | ||
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[[Category: Tsai, L C.]] | [[Category: Tsai, L C.]] | ||
[[Category: Yuan, H S.]] | [[Category: Yuan, H S.]] | ||
| - | [[Category: CA]] | ||
[[Category: circular-permutated jellyroll protein]] | [[Category: circular-permutated jellyroll protein]] | ||
| - | ''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 22:21:37 2008'' |
Revision as of 19:21, 30 March 2008
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| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Licheninase, with EC number 3.2.1.73 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
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
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