1N97: Crystal Structure Of Cyp175a1 From Thermus Thermophillus Strain Hb27

Citation:
Abstract
The second structure of a thermophile cytochrome P450, CYP175A1 from the thermophilic bacterium Thermus thermophilus HB27, has been solved to 1.8-A resolution. The overall P450 structure remains conserved despite the low sequence identity between the various P450s. The CYP175A1 structure lacks the large aromatic network found in the only other thermostable P450, CYP119, thought to contribute to thermal stability. The primary difference between CYP175A1 and its mesophile counterparts is the investment of charged residues into salt-link networks at the expense of single charge-charge interactions. Additional factors involved in the thermal stability increase are a decrease in the overall size, especially shortening of loops and connecting regions, and a decrease in the number of labile residues such as Asn, Gln, and Cys.
PDB ID: 1N97Download
MMDB ID: 22100
PDB Deposition Date: 2002/11/22
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 1N97: monomeric; determined by author
Molecular Components in 1N97
Label Count Molecule
Protein (1 molecule)
1
Cyp175a1
Molecule annotation
Chemicals (9 molecules)
1
1
2
1
3
7
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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