4AE5

STRUCTURE OF A MAJOR REGULATOR OF STAPHYLOCOCCAL PATHOGENESIS

PDB DOI: https://doi.org/10.2210/pdb4AE5/pdb

Classification: SIGNALING PROTEIN
Organism(s): Staphylococcus aureus
Mutation(s): No

Deposited: 2012-01-08 Released: 2012-07-04
Deposition Author(s): Hirshberg, M., Henrick, K.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.85 Å
R-Value Free: 0.260
R-Value Work: 0.211
R-Value Observed: 0.214

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Structure of the Signal Transduction Protein Trap (Target of Rnaiii-Activating Protein).

Henrick, K., Hirshberg, M.

(2012) Acta Crystallogr Sect F Struct Biol Cryst Commun 68: 744

PubMed: 22750855 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1107/S1744309112020167
Primary Citation of Related Structures:
4AE5

PubMed Abstract:
The crystal structure of the signal transduction protein TRAP is reported at 1.85 Å resolution. The structure of TRAP consists of a central eight-stranded β-barrel flanked asymmetrically by helices and is monomeric both in solution and in the crystal structure. A formate ion was found bound to TRAP identically in all four molecules in the asymmetric unit.

Organizational Affiliation

Research Collaboratory for Structural Bioinformatics Protein Data Bank, Department of Chemistry and Chemical Biology, Rutgers, The State University of New Jersey, 610 Taylor Road, Piscataway, NJ 08854-8087, USA.

Macromolecule Content

Total Structure Weight: 78.48 kDa
Atom Count: 5,678
Modelled Residue Count: 639
Deposited Residue Count: 668
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
SIGNAL TRANSDUCTION PROTEIN TRAP	A, B, C, D	167	Staphylococcus aureus	Mutation(s): 0
UniProt
Find proteins for Q2G2F3 (Staphylococcus aureus (strain NCTC 8325 / PS 47)) Explore Q2G2F3 Go to UniProtKB: Q2G2F3
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q2G2F3
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 1 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FMT Query on FMT Download Ideal Coordinates CCD File SDF format, chain G [auth C] SDF format, chain E [auth A] SDF format, chain F [auth B] SDF format, chain H [auth D] MOL2 format, chain G [auth C] MOL2 format, chain E [auth A] MOL2 format, chain F [auth B] MOL2 format, chain H [auth D]	E [auth A], F [auth B], G [auth C], H [auth D]	FORMIC ACID C H₂ O₂ BDAGIHXWWSANSR-UHFFFAOYSA-N		Interactions Focus chain E [auth A] Focus chain F [auth B] Focus chain G [auth C] Focus chain H [auth D] Interactions & Density Focus chain E [auth A] Focus chain F [auth B] Focus chain G [auth C] Focus chain H [auth D]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.85 Å
R-Value Free: 0.260
R-Value Work: 0.211
R-Value Observed: 0.214
Space Group: P 1 2₁ 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 69.076	α = 90
b = 70.868	β = 111.53
c = 79.082	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
DENZO	data reduction
SCALEPACK	data scaling
PHENIX	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2012-07-04

Deposition Author(s):

Hirshberg, M.

Henrick, K.

Revision History (Full details and data files)

Version 1.0: 2012-07-04
Type: Initial release
Version 1.1: 2012-07-11
Changes: Other
Version 1.2: 2019-05-08
Changes: Data collection, Experimental preparation, Other