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PDBsum entry 4qa8

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protein ligands links
Lipid transport PDB id
4qa8

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
210 a.a.
Ligands
PJZ
Waters ×156
PDB id:
4qa8
Name: Lipid transport
Title: Crystal structure of lprf from mycobacterium bovis
Structure: Putative lipoprotein lprf. Chain: a. Fragment: unp residues 40-261. Engineered: yes
Source: Mycobacterium bovis. Organism_taxid: 233413. Strain: atcc baa-935 / af2122/97. Gene: lprf, mb1403. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.10Å     R-factor:   0.165     R-free:   0.189
Authors: N.C.Ha,L.Jiao,J.S.Kim
Key ref: J.S.Kim et al. (2014). Crystal structure and functional implications of LprF from Mycobacterium tuberculosis and M. bovis. Acta Crystallogr D Biol Crystallogr, 70, 2619-2630. PubMed id: 25286846 DOI: 10.1107/S1399004714016599
Date:
02-May-14     Release date:   22-Oct-14    
PROCHECK
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 Headers
 References

Protein chain
P65315  (LPRF_MYCBO) -  Putative diacylated glycolipid transporter LprF from Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Seq:
Struc:
261 a.a.
210 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1107/S1399004714016599 Acta Crystallogr D Biol Crystallogr 70:2619-2630 (2014)
PubMed id: 25286846  
 
 
Crystal structure and functional implications of LprF from Mycobacterium tuberculosis and M. bovis.
J.S.Kim, L.Jiao, J.I.Oh, N.C.Ha, Y.H.Kim.
 
  ABSTRACT  
 
The Gram-positive bacteria Mycobacterium tuberculosis and M. bovis are causative agents of tuberculosis in humans and cattle. The lipoprotein LprF is found in M. tuberculosis and M. bovis but not in the nonpathogenic M. smegmatis. To date, the role of LprF remains to be elucidated. In this study, the crystal structure of LprF has been determined at 1.1 Å resolution. The overall structure is similar to that of a homologue, LprG, with a central hydrophobic cavity that binds a triacylated glycolipid. LprF exhibited a central cavity structure similar to that of LprG, but with a smaller cavity that binds two alkyl chains. Consistently, subsequent mass-spectrometric analysis revealed that the bound ligand was a diacylated glycolipid, as found in the structure. Furthermore, an increased ratio of lipoarabinomannan to lipomannan in the mycobacterial cell wall was observed when lprF was introduced into M. smegmatis. These observations suggested that LprF transfers the diacylated glycolipid from the plasma membrane to the cell wall, which might be related to the pathogenesis of the bacteria.
 

 

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