1NSW

The Crystal Structure of the K18G Mutant of the thioredoxin from Alicyclobacillus acidocaldarius

PDB DOI: https://doi.org/10.2210/pdb1NSW/pdb

Classification: ELECTRON TRANSPORT
Organism(s): Alicyclobacillus acidocaldarius
Expression System: Escherichia coli
Mutation(s): Yes

Deposited: 2003-01-28 Released: 2003-08-05
Deposition Author(s): Bartolucci, S., De Simone, G., Galdiero, S., Improta, R., Menchise, V., Pedone, C., Pedone, E., Saviano, M.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.249
R-Value Work: 0.205
R-Value Observed: 0.237

wwPDB Validation 3D Report Full Report

This is version 1.4 of the entry. See complete history.

Literature

An integrated structural and computational study of the thermostability of two thioredoxin mutants from Alicyclobacillus acidocaldarius

Bartolucci, S., De Simone, G., Galdiero, S., Improta, R., Menchise, V., Pedone, C., Pedone, E., Saviano, M.

(2003) J Bacteriol 185: 4285-4289

PubMed: 12837806 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1128/JB.185.14.4285-4289.2003
Primary Citation of Related Structures:
1NSW, 1NW2

PubMed Abstract:
We report a crystallographic and computational analysis of two mutant forms of the Alicyclobacillus acidocaldarius thioredoxin (BacTrx) done in order to evaluate the contribution of two specific amino acids to the thermostability of BacTrx. Our results suggest that the thermostability of BacTrx may be modulated by mutations affecting the overall electrostatic energy of the protein.

Organizational Affiliation

Dipartimento di Chimica Biologica, University of Naples Federico II, Istituto di Biostrutture e Bioimmagini-CNR, 80134 Naples, Italy.

Macromolecule Content

Total Structure Weight: 46.05 kDa
Atom Count: 3,470
Modelled Residue Count: 420
Deposited Residue Count: 420
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
THIOREDOXIN	A, B, C, D	105	Alicyclobacillus acidocaldarius	Mutation(s): 1 EC: 1.8.1.9
UniProt
Find proteins for P80579 (Alicyclobacillus acidocaldarius subsp. acidocaldarius) Explore P80579 Go to UniProtKB: P80579
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P80579
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.90 Å
R-Value Free: 0.249
R-Value Work: 0.205
R-Value Observed: 0.237
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 46.73	α = 90
b = 73.89	β = 103.79
c = 54.91	γ = 90

Software Package:

Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
AMoRE	phasing
CNS	refinement

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2003-08-05

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2003-08-05
Type: Initial release
Version 1.1: 2008-04-29
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2021-10-27
Changes: Data collection, Database references
Version 1.4: 2023-08-16
Changes: Data collection, Refinement description

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.