2004
DOI: 10.1110/ps.03532204
|View full text |Cite
|
Sign up to set email alerts
|

NMR structure of the noncytotoxic α‐sarcin mutant Δ(7‐22): The importance of the native conformation of peripheral loops for activity

Abstract: The deletion mutant ⌬(7-22) of ␣-sarcin, unlike its wild-type protein counterpart, lacks the specific ability to degrade rRNA in intact ribosomes and exhibits an increased unspecific ribonuclease activity and decreased interaction with lipid vesicles. In trying to shed light on these differences, we report here on the three-dimensional structure of the ⌬(7-22) ␣-sarcin mutant using NMR methods. We also evaluated its dynamic properties on the basis of theoretical models and measured its correlation time (6.2 ns… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

4
33
0

Year Published

2005
2005
2018
2018

Publication Types

Select...
4
1
1

Relationship

0
6

Authors

Journals

citations
Cited by 16 publications
(37 citation statements)
references
References 47 publications
4
33
0
Order By: Relevance
“…This involvement might be in terms of a direct interaction with the polymer or most probably due to a modification of the active site accessibility, as has been also suggested before [15,51]. In fact, these solvent accessibility changes were detected before upon deletion of the β-hairpin [22].…”
Section: Discussionsupporting
confidence: 56%
See 1 more Smart Citation
“…This involvement might be in terms of a direct interaction with the polymer or most probably due to a modification of the active site accessibility, as has been also suggested before [15,51]. In fact, these solvent accessibility changes were detected before upon deletion of the β-hairpin [22].…”
Section: Discussionsupporting
confidence: 56%
“…An α-sarcin mutant involving the deletion of this protuberance, α-sarcin Δ (7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20)(21)(22), retained the same conformation as the wildtype protein, as ascertained from its three-dimensional structure in solution [22].…”
Section: Introductionmentioning
confidence: 96%
“…One of them was the wild-type major A. fumigatus allergen Asp f 1 (García-Ortega et al, 2005). Two other ones were the corresponding Δ(7-22) deleted variants of Asp f 1 and α-sarcin, two proteins with highly reduced IgE-reactivity and citotoxicity (García-Ortega et al, 2002García-Mayoral et al, 2004). The fourth one (H137Q) was a mutant version of α-sarcin where only the catalytically essential His-137 has been mutated, being substituted by Gln (Lacadena et al, 1995).…”
Section: Production Of the Other Allergenic Variantsmentioning
confidence: 99%
“…The second of them (residues 7-22) juts out as a solvent-exposed protuberance and is one of the protein regions with highest conformational flexibility (Pérez-Cañadillas et al, 2000, 2002. Deletion of this β-sheet results in a Δ(7-22) mutant that shows no significant conformational differences except for the deleted region (García-Mayoral et al, 2004) but has lost its ability to specifically recognize the ribosome and is much less cytotoxic (García-Ortega et al, 2002).…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation