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PDBsum entry 4rvc

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protein links
Transport protein PDB id
4rvc

 

 

 

 

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Contents
Protein chain
240 a.a.
Waters ×206
PDB id:
4rvc
Name: Transport protein
Title: Structure of atp binding subunit of abc transporter
Structure: Abc transporter atp-binding protein. Chain: a. Fragment: unp residues 13-257. Engineered: yes
Source: Geobacillus kaustophilus. Organism_taxid: 1337888. Strain: gblys. Gene: gbl_2030. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.77Å     R-factor:   0.216     R-free:   0.250
Authors: M.Manjula,K.J.Pampa,N.K.Lokanath
Key ref: M.Manjula et al. (2015). Crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus. Biochem Biophys Res Commun, 459, 113-117. PubMed id: 25724946 DOI: 10.1016/j.bbrc.2015.02.079
Date:
26-Nov-14     Release date:   18-Mar-15    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
U2YAF6  (U2YAF6_GEOKU) -  ABC transporter ATP-binding protein from Geobacillus kaustophilus GBlys
Seq:
Struc:
257 a.a.
240 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1016/j.bbrc.2015.02.079 Biochem Biophys Res Commun 459:113-117 (2015)
PubMed id: 25724946  
 
 
Crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus.
M.Manjula, K.J.Pampa, S.M.Kumar, S.Mukherjee, N.Kunishima, K.S.Rangappa, N.K.Lokanath.
 
  ABSTRACT  
 
The ATP binding cassette (ABC) transporters, represent one of the largest superfamilies of primary transporters, which are very essential for various biological functions. The crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus has been determined at 1.77 Å resolution. The crystal structure revealed that the protomer has two thick arms, (arm I and II), which resemble 'L' shape. The ATP-binding pocket is located close to the end of arm I. ATP molecule is docked into the active site of the protein. The dimeric crystal structure of ATP-binding subunit of ABC transporter from G. kaustophilus has been compared with the previously reported crystal structure of ATP-binding subunit of ABC transporter from Salmonella typhimurium.
 

 

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