 |

*
Residue conservation analysis
|
|
| PDB id: |
 |
3b7m
|
 |
| Name: |
 |
Hydrolase
|
 |
| Title: |
 |
Crystal structure of a meso-active thermo-stable cellulase (mt cel12a) derived by making non-contiguous mutations in the active surface of the cel12a cellulase of rhodothermus marinus
|
 |
 Structure: |
 |
Cellulase. Chain: a, b, c, d. Engineered: yes
|
 |

Source:
|
 |
Rhodothermus marinus. Organism_taxid: 29549. Gene: cela. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
 |

UniProt:
|
 |
|
Chains A,
B,
C,
D:
O33897
(O33897_RHOMR)
|
| Seq: |
 |
 |
 |
260 a.a. |
|
| Struc: |
216 a.a.* |
 |
 |
 |
| Key: |
 |
PfamA domain |
 |
 |
 |
 |
Secondary structure |
 |
 |
CATH domain |
 |
|
|
 |
|
* PDB and UniProt seqs differ
at 50 residue positions (black
crosses)
|
|
 |

Enzyme class:
|
 |
|
 |

Reaction:
|
 |
Endohydrolysis of 1,4-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
|
 |
 |

Resolution:
|
 |
2.10Å
|
 |

R-factor:
|
 |
0.189
|
 |

R-free:
|
 |
0.238
|
 |

Authors:
|
 |
S.Karthikeyan,P.Guptasarma
|
 |

Key ref:
|
 |
d.kapoor
et al.
Transplantation of the active surface of a mesophile cellulase onto the structural scaffold of a homologous thermophile cellulase through engineering of a surface beta sheet.
To be Published,
xsi:nil="true" />.
|
 |

Date:
|
 |
31-Oct-07
|
 |

Release date:
|
 |
27-Nov-07
|
 |

Related entries:
|
 |
crystal structure of rhodothermus marinus cel12a
crystal structure of trichoderma reesei cel12a
|
 |
|
|
|
 |
Quick_links |
 |
 |
Procheck |
 |
 |
Surface |
 |
|
|