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PDBsum entry 2ith
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Oxidoreductase PDB id
2ith

 

 

 

 

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Contents
Protein chain
162 a.a. *
* Residue conservation analysis
PDB id:
2ith
Name: Oxidoreductase
Title: Nmr structure of haloferax volcanii dhfr
Structure: Dihydrofolate reductase. Chain: a. Engineered: yes
Source: Haloferax volcanii. Organism_taxid: 2246. Gene: fola. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: B.Binbuga
Key ref:
B.Binbuga et al. (2007). Structure in an extreme environment: NMR at high salt. Protein Sci, 16, 1783-1787. PubMed id: 17656587 DOI: 10.1110/ps.072950407
Date:
19-Oct-06     Release date:   04-Sep-07    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P15093  (DYRA_HALVD) -  Dihydrofolate reductase HdrA from Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)
Seq:
Struc: 		162 a.a.
162 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.1.5.1.3  - dihydrofolate reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Folate Coenzymes
      Reaction: (6S)-5,6,7,8-tetrahydrofolate + NADP+ = 7,8-dihydrofolate + NADPH + H+
(6S)-5,6,7,8-tetrahydrofolate
 + NADP(+)
 = 7,8-dihydrofolate
 + NADPH
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1110/ps.072950407 Protein Sci 16:1783-1787 (2007)
PubMed id: 17656587  
 
 
Structure in an extreme environment: NMR at high salt.
B.Binbuga, A.F.Boroujerdi, J.K.Young.
 
  ABSTRACT  
 
Proteins from halophiles have adapted to challenging environmental conditions and require salt for their structure and function. How halophilic proteins adapted to a hypersaline environment is still an intriguing question. It is important to mimic the physiological conditions of the archae extreme halophiles when characterizing their enzymes, including structural characterization. The NMR derived structure of Haloferax volcanii dihydrofolate reductase in 3.5 M NaCl is presented, and represents the first high salt structure calculated using NMR data. Structure calculations show that this protein has a solution structure which is similar to the previously determined crystal structure with a difference at the N terminus of beta3 and the type of beta-turn connection beta7 and beta8.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. (A) Backbone superimposition of the 20 lowest energy structures of hvDHFR1, and (B) a representative structure generated
 
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2007, 16, 1783-1787) copyright 2007.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
18825778 A.F.Boroujerdi, and J.K.Young (2009).
NMR-derived folate-bound structure of dihydrofolate reductase 1 from the halophile Haloferax volcanii.
  Biopolymers, 91, 140-144.
PDB code: 2jyb
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

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