spacer
spacer

PDBsum entry 5avd

Go to PDB code: 
protein ligands links
Isomerase PDB id
5avd

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
240 a.a.
Ligands
SO4 ×2
Waters ×324
PDB id:
5avd
Name: Isomerase
Title: The 0.86 angstrom structure of elastase crystallized in high-strength agarose hydrogel
Structure: Chymotrypsin-like elastase family member 1. Chain: a. Synonym: elastase-1. Engineered: yes
Source: Sus scrofa. Pig. Organism_taxid: 9823. Gene: cela1, ela1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
0.86Å     R-factor:   0.129     R-free:   0.140
Authors: S.Sugiyama,N.Shimizu,M.Maruyama,G.Sazaki,H.Adachi,K.Takano, S.Murakami,T.Inoue,Y.Mori,H.Matsumura
Key ref: S.Sugiyama et al. (2012). Growth of protein crystals in hydrogels prevents osmotic shock. J Am Chem Soc, 134, 5786-5789. PubMed id: 22435400
Date:
15-Jun-15     Release date:   08-Jul-15    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00772  (CELA1_PIG) -  Chymotrypsin-like elastase family member 1 from Sus scrofa
Seq:
Struc:
266 a.a.
240 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.3.4.21.36  - pancreatic elastase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.

 

 
J Am Chem Soc 134:5786-5789 (2012)
PubMed id: 22435400  
 
 
Growth of protein crystals in hydrogels prevents osmotic shock.
S.Sugiyama, M.Maruyama, G.Sazaki, M.Hirose, H.Adachi, K.Takano, S.Murakami, T.Inoue, Y.Mori, H.Matsumura.
 
  ABSTRACT  
 
High-throughput protein X-ray crystallography offers a significant opportunity to facilitate drug discovery. The most reliable approach is to determine the three-dimensional structure of the protein-ligand complex by soaking the ligand in apo crystals. However, protein apo crystals produced by conventional crystallization in a solution are fatally damaged by osmotic shock during soaking. To overcome this difficulty, we present a novel technique for growing protein crystals in a high-concentration hydrogel that is completely gellified and exhibits high strength. This technique allowed us essentially to increase the mechanical stability of the crystals, preventing serious damage to the crystals caused by osmotic shock. Thus, this method may accelerate structure-based drug discoveries.
 

 

spacer

spacer