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PDBsum entry 3vnd

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protein ligands Protein-protein interface(s) links
Lyase PDB id
3vnd
Jmol
Contents
Protein chains
(+ 2 more) 259 a.a.
Ligands
SO4 ×18
PE8 ×4
Waters ×1187
PDB id:
3vnd
Name: Lyase
Title: Crystal structure of tryptophan synthase alpha-subunit from psychrophile shewanella frigidimarina k14-2
Structure: Tryptophan synthase alpha chain. Chain: a, b, c, d, e, f, g, h. Synonym: tsa. Engineered: yes
Source: Shewanella frigidimarina. Organism_taxid: 56812. Strain: k14-2. Gene: trpa. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.60Å     R-factor:   0.175     R-free:   0.211
Authors: D.Mitsuya,S.Tanaka,H.Matsumura,K.Takano,N.Urano,M.Ishida
Key ref: D.Mitsuya et al. (2014). Strategy for cold adaptation of the tryptophan synthase α subunit from the psychrophile Shewanella frigidimarina K14-2: crystal structure and physicochemical properties. J Biochem, 155, 73-82. PubMed id: 24163283 DOI: 10.1093/jb/mvt098
Date:
12-Jan-12     Release date:   16-Jan-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
H1AFK5  (H1AFK5_SHEFR) -  Tryptophan synthase alpha chain
Seq:
Struc:
267 a.a.
259 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     3 terms  

 

 
DOI no: 10.1093/jb/mvt098 J Biochem 155:73-82 (2014)
PubMed id: 24163283  
 
 
Strategy for cold adaptation of the tryptophan synthase α subunit from the psychrophile Shewanella frigidimarina K14-2: crystal structure and physicochemical properties.
D.Mitsuya, S.Tanaka, H.Matsumura, N.Urano, K.Takano, K.Ogasahara, M.Takehira, K.Yutani, M.Ishida.
 
  ABSTRACT  
 
To investigate the molecular basis of cold adaptation of enzymes, we determined the crystal structure of the tryptophan synthase α subunit (SfTSA) from the psychrophile Shewanella frigidimarina K14-2 by X-ray analysis at 2.6-Å resolution and also examined its physicochemical properties. SfTSA was found to have the following characteristics: (i) The stabilities against heat and denaturant of SfTSA were lower than those of an α subunit (EcTSA) from Escherichia coli. This lower equilibrium stability originated from both a faster unfolding rate and a slower refolding rate; (ii) the heat denaturation of SfTSA was completely reversible at pH 7.0 and the solubility of denatured SfTSA was higher than that of denatured EcTSA. The two-state transition of denaturation for SfTSA was highly cooperative, whereas the denaturation process of EcTSA was considerably more complex and (iii) the global structure of SfTSA was quite similar to those of α subunits from other species. Relative to those other proteins, SfTSA exhibited an increase in cavity volume and a decrease in the number of ion pairs. SfTSA also lacks a hydrogen bond near loop B, related to catalytic function. These characteristics of SfTSA might provide the conformational flexibility required for catalytic activity at low temperatures.