Reversible unfolding and refolding behavior of a monomeric aldolase from Staphylococcus aureus.


Abstract

Thermal and GdmCl-induced unfolding transitions of aldolase from Staphylococcus aureus are reversible under a variety of solvent conditions. Analysis of the transitions reveals that no partially folded intermediates can be detected under equilibrium conditions. The stability of the enzyme is very low with a delta G0 value of -9 +/- 2 kJ/mol at 20 degrees C. The kinetics of unfolding and refolding of aldolase are complex and comprise at least one fast and two slow reactions. This complexity arises from prolyl isomerization reactions in the unfolded chain, which are kinetically coupled to the actual folding reaction. Comparison with model calculations shows that at least two prolyl peptide bonds give rise to the observed slow folding reactions of aldolase and that all of the involved bonds are presumably in the trans conformation in the native state. The rate constant of the actual folding reaction is fast with a relaxation time of about 15 s at the midpoint of the folding transition at 15 degrees C. The data presented on the folding and stability of aldolase are comparable to the properties of much smaller proteins. This might be connected with the simple and highly repetitive tertiary structure pattern of the enzyme, which belongs to the group of alpha/beta barrel proteins. Study holds ProTherm entries: 10588, 10589, 10590 Extra Details: alpha/beta barrel; folding intermediate; prolyl isomerization;,protein folding kinetics; two-state model

Submission Details

ID: z7FkTed24

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:40 p.m.

Version: 1

Publication Details
Rudolph R;Siebendritt R;Kiefhaber T,Protein Sci. (1992) Reversible unfolding and refolding behavior of a monomeric aldolase from Staphylococcus aureus. PMID:1304364
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
1DHN 1999-04-20 1.65 1.65 ANGSTROM RESOLUTION STRUCTURE OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS
2NM3 2007-09-04 1.68 Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2S)-monapterin at 1.68 angstrom resolution
2NM2 2007-09-04 1.7 Crystal structure of dihydroneopterin aldolase from S. aureus in complex with (1S,2R)-neopterin at 1.50 Angstrom resolution
1RRI 2004-03-30 2.0 DHNA complex with 3-(5-amino-7-hydroxy-[1,2,3] triazolo [4,5-d]pyrimidin-2-yl)-benzoic acid
1RSI 2004-03-30 2.2 DHNA complex with 2-Amino-5-bromo-3-hydroxy-6-phenylpyrimidine
2DHN 1999-04-20 2.2 COMPLEX OF 7,8-DIHYDRONEOPTERIN ALDOLASE FROM STAPHYLOCOCCUS AUREUS WITH 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 2.2 A RESOLUTION
1RRW 2004-03-30 2.21 DHNA complexed with 9-methylguanine
1RS2 2004-03-30 2.31 DHNA complex with 8-Amino-1,3-dimethyl-3,7-dihydropurine-2,6-dione
1U68 2004-10-19 2.4 DHNA 7,8 DIHYDRONEOPTERIN COMPLEX
1RSD 2004-03-30 2.5 DHNA complex with 3-(5-Amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-[2-(2-hydroxymethyl-phenylsulfanyl)-benzyl]-benzamide
1RS4 2004-03-30 2.7 DHNA, 7,8-Dihydroneopterin Aldolase complexed with 3-(5-Amino-7-hydroxy-[1,2,3]triazolo[4,5-d]pyrimidin-2-yl)-N-(3,5-dichlorobenzyl)-benzamide
1RRY 2004-03-30 2.7 DHNA complexed with 2-amino-4-hydroxy-5-carboxyethylpyrimidine

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
99.2 Dihydroneopterin aldolase P64147 FOLB_STAAW
99.2 Dihydroneopterin aldolase Q6GBX3 FOLB_STAAS
99.2 Dihydroneopterin aldolase P64146 FOLB_STAAN
99.2 Dihydroneopterin aldolase P64145 FOLB_STAAM
99.2 Dihydroneopterin aldolase Q5HIG0 FOLB_STAAC
100.0 Dihydroneopterin aldolase P56740 FOLB_STAAU
100.0 Dihydroneopterin aldolase Q6GJF6 FOLB_STAAR