spacer
spacer

PDBsum entry 2w8h

Go to PDB code: 
protein ligands metals Protein-protein interface(s) links
Membrane protein PDB id
2w8h

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
(+ 2 more) 322 a.a. *
Ligands
MTN ×8
Metals
_CL
Waters ×13
* Residue conservation analysis
PDB id:
2w8h
Name: Membrane protein
Title: Crystal structure of spin labeled wza24-345.
Structure: Putative outer membrane lipoprotein wza. Chain: a, b, c, d, e, f, g, h. Fragment: periplasmic domain, residues 22-345. Synonym: wza. Engineered: yes. Mutation: yes. Other_details: labeled with mtssl at postion 335
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.76Å     R-factor:   0.212     R-free:   0.229
Authors: G.Hagelueken,W.J.Ingledew,H.Huang,B.Petrovic-Stojanovska,C.Whitfield, H.Elmkami,O.Schiemann,J.H.Naismith
Key ref: G.Hagelueken et al. (2009). PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein Wza from Escherichia coli. Angew Chem Int Ed Engl, 48, 2904-2906. PubMed id: 19294709
Date:
16-Jan-09     Release date:   10-Feb-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9X4B7  (Q9X4B7_ECOLX) -  Putative outer membrane lipoprotein Wza from Escherichia coli
Seq:
Struc:
379 a.a.
322 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
Angew Chem Int Ed Engl 48:2904-2906 (2009)
PubMed id: 19294709  
 
 
PELDOR spectroscopy distance fingerprinting of the octameric outer-membrane protein Wza from Escherichia coli.
G.Hagelueken, W.J.Ingledew, H.Huang, B.Petrovic-Stojanovska, C.Whitfield, H.ElMkami, O.Schiemann, J.H.Naismith.
 
  ABSTRACT  
 
Distance fingerprinting: Pulsed electron-electron double resonance spectroscopy (PELDOR) is applied to the octameric membrane protein complex Wza of E. coli. The data yielded a detailed distance fingerprint of its periplasmic region that compares favorably to the crystal structure. These results provide the foundation to study conformation changes from interaction with partner proteins.
 

 

spacer

spacer