Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro.


Abstract

The folding of maltose-binding protein, a periplasmic protein in Escherichia coli, was shown to proceed through the same rate-limiting step whether folding occurred in the cell under physiological conditions or in vitro in the absence of other proteins. Four species of maltose-binding protein containing aminoacyl substitutions identified as decreasing the rate of folding of the protein in vivo were purified, and their denaturant-induced folding transitions were analyzed by monitoring the intrinsic fluorescence of tryptophan. In all four cases the rate of folding in vitro was slower than that of the wild-type maltose-binding protein; thus the same step determines the rate of folding in vivo and in vitro. Furthermore, examination of the three-dimensional structure of maltose-binding protein as determined by x-ray crystallography (F. Quiocho, personal communication; Spurlino, J. C., Lu, G.-Y., and Quiocho, F. A. (1991) J. Biol. Chem. 266, 5202-5219) indicates that all 4 of the residues identified as crucial to folding lie in one structural element of the native protein. We conclude that the rate-limiting step both in vivo and in vitro involves formation of this element of structure. Study holds ProTherm entries: 5226, 5227, 5228, 5229, 5230, 5231, 5232 Extra Details: periplasmic protein; rate-limiting step; folding transitions;,structural element

Submission Details

ID: ADyrbQZt3

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:29 p.m.

Version: 1

Publication Details
Chun SY;Strobel S;Bassford P;Randall LL,J. Biol. Chem. (1993) Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro. PMID:8407916
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
3JYR 2009-09-22T00:00:00+0000 1.75 Crystal structures of the GacH receptor of Streptomyces glaucescens GLA.O in the unliganded form and in complex with acarbose and an acarbose homolog. Comparison with acarbose-loaded maltose binding protein of Salmonella typhimurium.
6L0Z 2019-09-27T00:00:00+0000 1.6 The crystal structure of Salmonella enterica sugar-binding protein MalE
6L3E 2019-10-10T00:00:00+0000 1.6 Crystal structure of Salmonella enterica sugar-binding protein MalE
3IO4 2009-08-13T00:00:00+0000 3.63 Huntingtin amino-terminal region with 17 Gln residues - Crystal C90
3OSQ 2010-09-09T00:00:00+0000 1.9 Maltose-bound maltose sensor engineered by insertion of circularly permuted green fluorescent protein into E. coli maltose binding protein at position 175
3OSR 2010-09-09T00:00:00+0000 2.0 Maltose-bound maltose sensor engineered by insertion of circularly permuted green fluorescent protein into E. coli maltose binding protein at position 311
3VD8 2012-01-04T00:00:00+0000 2.07 Crystal structure of human AIM2 PYD domain with MBP fusion
4FEB 2012-05-29T00:00:00+0000 2.8 Crystal Structure of Htt36Q3H-EX1-X1-C2(Beta)
4MY2 2013-09-27T00:00:00+0000 2.4 Crystal Structure of Norrin in fusion with Maltose Binding Protein
4WGI 2014-09-18T00:00:00+0000 1.85 A Single Diastereomer of a Macrolactam Core Binds Specifically to Myeloid Cell Leukemia 1 (MCL1)

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
90.7 Maltose-binding periplasmic protein P41130 MALE_PHOLU
93.9 Maltose-binding periplasmic protein P18815 MALE_KLEAE
94.3 Maltose-binding periplasmic protein P19576 MALE_SALTY
100.0 Maltose-binding periplasmic protein P0AEX9 MALE_ECOLI
100.0 Maltose-binding periplasmic protein P0AEY0 MALE_ECO57