Thermostability of cytochrome c-552 from the thermophilic hydrogen-oxidizing bacterium Hydrogenobacter thermophilus.


Abstract

The denaturation of the c-type cytochrome of the thermophilic bacterium Hydrogenobacter thermophilus cytochrome c-552 by heat and guanidine hydrochloride was studied by measuring the change in circular dichroic spectra. The melting temperature (T1/2) of cytochrome c-552 in the presence of 1.5 M guanidine hydrochloride was 34 degrees C higher than that of the c-type cytochrome of Pseudomonas aeruginosa cytochrome c-551. Hydrogenobacter cytochrome c-552 is a much more stable protein than cytochrome c-551 of the mesophilic bacterium P. aeruginosa, even though their amino acid sequences are 56% identical and they have numerous other similarities. However, notwithstanding these similarities between the sequences of the cytochromes c-552 and c-551 that were compared, it is very likely that these differences in stability could be due to some heretofore undefined differences in their spatial structures. It has been suggested that alpha-helix structure and electrostatic interaction could be the source of the stable spatial structure of cytochrome c-552. Study holds ProTherm entries: 3858, 3859, 3860, 3861, 3862, 3863, 3864, 3865 Extra Details: In the presence of 1.5M GdnHCl thermophilic hydrogen-oxidizing bacterium; spatial structures;,alpha-helix structure; electrostatic interaction

Submission Details

ID: dwQLaSA9

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:23 p.m.

Version: 1

Publication Details
Sanbongi Y;Igarashi Y;Kodama T,Biochemistry (1989) Thermostability of cytochrome c-552 from the thermophilic hydrogen-oxidizing bacterium Hydrogenobacter thermophilus. PMID:2558725
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
2PAC 1993-10-31 SOLUTION STRUCTURE OF FE(II) CYTOCHROME C551 FROM PSEUDOMONAS AERUGINOSA AS DETERMINED BY TWO-DIMENSIONAL 1H NMR
1DVV 2000-11-29 SOLUTION STRUCTURE OF THE QUINTUPLE MUTANT OF CYTOCHROME C-551 FROM PSEUDOMONAS AERUGINOSA
2AI5 2006-05-23 Solution Structure of Cytochrome C552, determined by Distributed Computing Implementation for NMR data
1AYG 1998-11-25 SOLUTION STRUCTURE OF CYTOCHROME C-552, NMR, 20 STRUCTURES
5XEC 2017-08-09 1.1 Heterodimer constructed from PA cyt c551-HT cyt c552 and HT cyt c552-PA cyt c551 chimeric proteins
5AUR 2015-10-21 1.26 Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at N-terminal region
5AUS 2015-10-21 1.3 Hydrogenobacter thermophilus cytochrome c552 dimer formed by domain swapping at C-terminal region
3X39 2015-04-22 1.5 Domain-swapped dimer of Pseudomonas aeruginosa cytochrome c551
5XED 2017-08-09 1.55 Heterodimer constructed from M61A PA cyt c551-HT cyt c552 and HT cyt c552-PA cyt c551 chimeric proteins
451C 1981-10-02 1.6 STRUCTURE OF CYTOCHROME C551 FROM P. AERUGINOSA REFINED AT 1.6 ANGSTROMS RESOLUTION AND COMPARISON OF THE TWO REDOX FORMS
351C 1981-10-02 1.6 STRUCTURE OF CYTOCHROME C551 FROM P. AERUGINOSA REFINED AT 1.6 ANGSTROMS RESOLUTION AND COMPARISON OF THE TWO REDOX FORMS
4ZID 2016-02-10 1.8 Dimeric Hydrogenobacter thermophilus cytochrome c552 obtained from Escherichia coli
2EXV 2006-02-07 1.86 Crystal structure of the F7A mutant of the cytochrome c551 from Pseudomonas aeruginosa
3VYM 2012-11-07 2.0 Dimeric Hydrogenobacter thermophilus cytochrome c552
1YNR 2005-05-17 2.0 Crystal structure of the cytochrome c-552 from Hydrogenobacter thermophilus at 2.0 resolution

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Cytochrome c-552 P15452 CY552_HYDTT
100.0 Cytochrome c-551 P00099 CY551_PSEAE