3UOR

The structure of the sugar-binding protein MalE from the phytopathogen Xanthomonas citri

PDB DOI: https://doi.org/10.2210/pdb3UOR/pdb

Classification: SUGAR BINDING PROTEIN
Organism(s): Xanthomonas citri pv. citri str. 306
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2011-11-17 Released: 2011-12-14
Deposition Author(s): Medrano, F.J., Souza, C.S., Balan, A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.20 Å
R-Value Free: 0.228
R-Value Work: 0.189
R-Value Observed: 0.191

wwPDB Validation 3D Report Full Report

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

Literature

Structure determination of a sugar-binding protein from the phytopathogenic bacterium Xanthomonas citri.

Medrano, F.J., de Souza, C.S., Romero, A., Balan, A.

(2014) Acta Crystallogr Sect F Struct Biol Cryst Commun 70: 564-571

PubMed: 24817711 Search on PubMedSearch on PubMed Central
DOI: https://doi.org/10.1107/S2053230X14006578
Primary Citation of Related Structures:
3UOR

PubMed Abstract:
The uptake of maltose and related sugars in Gram-negative bacteria is mediated by an ABC transporter encompassing a periplasmic component (the maltose-binding protein or MalE), a pore-forming membrane protein (MalF and MalG) and a membrane-associated ATPase (MalK). In the present study, the structure determination of the apo form of the putative maltose/trehalose-binding protein (Xac-MalE) from the citrus pathogen Xanthomonas citri in space group P6522 is described. The crystals contained two protein molecules in the asymmetric unit and diffracted to 2.8 Å resolution. Xac-MalE conserves the structural and functional features of sugar-binding proteins and a ligand-binding pocket with similar characteristics to eight different orthologues, including the residues for maltose and trehalose interaction. This is the first structure of a sugar-binding protein from a phytopathogenic bacterium, which is highly conserved in all species from the Xanthomonas genus.

Organizational Affiliation

Department of Chemical and Physical Biology, Centro de Investigaciones Biologicas (CSIC), Madrid, Spain.

Macromolecule Content

Total Structure Weight: 102.77 kDa
Atom Count: 6,719
Modelled Residue Count: 792
Deposited Residue Count: 916
Unique protein chains: 1

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ABC transporter sugar binding protein	A, B	458	Xanthomonas citri pv. citri str. 306	Mutation(s): 0 Gene Names: malE, XAC2310
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.20 Å
R-Value Free: 0.228
R-Value Work: 0.189
R-Value Observed: 0.191
Space Group: P 6₅ 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 122.971	α = 90
b = 122.971	β = 90
c = 304.28	γ = 120

Software Package:

Software Name	Purpose
MxCuBE	data collection
SHARP	phasing
PHENIX	refinement
XDS	data reduction
SCALA	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2011-12-14

Deposition Author(s):

Revision History (Full details and data files)

Version 1.0: 2011-12-14
Type: Initial release
Version 1.1: 2014-05-14
Changes: Database references
Version 1.2: 2014-09-24
Changes: Database references
Version 1.3: 2017-11-08
Changes: Refinement description
Version 1.4: 2024-02-28
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.