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Oxidoreductase PDB id
3cxk
Jmol
Contents
Protein chains
131 a.a. *
Ligands
ACT ×2
Metals
_ZN ×2
Waters ×180
* Residue conservation analysis
PDB id:
3cxk
Name: Oxidoreductase
Title: 1.7 a crystal structure of methionine-r-sulfoxide reductase burkholderia pseudomallei: crystallization in a microfluidi card.
Structure: Methionine-r-sulfoxide reductase. Chain: a, b. Engineered: yes
Source: Burkholderia pseudomallei strain. Strain: 1710b. Gene: msrb, burps1710b_2458, yp_333853. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.70Å     R-factor:   0.167     R-free:   0.199
Authors: S.Lovell,C.Gerdts,B.Staker,D.Craigen,L.Stewart,Accelerated Technologies Center For Gene To 3d Structure (Atcg3d),Seatt Structural Genomics Center For Infectious Disease (Ssgcid)
Key ref:
C.J.Gerdts et al. (2008). The plug-based nanovolume Microcapillary Protein Crystallization System (MPCS). Acta Crystallogr D Biol Crystallogr, 64, 1116-1122. PubMed id: 19020349 DOI: 10.1107/S0907444908028060
Date:
24-Apr-08     Release date:   27-May-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q3JRF0  (MSRB_BURP1) -  Peptide methionine sulfoxide reductase MsrB
Seq:
Struc:
143 a.a.
131 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.1.8.4.12  - Peptide-methionine (R)-S-oxide reductase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L- methionine (R)-S-oxide + thioredoxin
Peptide-L-methionine
+ thioredoxin disulfide
+ H(2)O
= peptide-L- methionine (R)-S-oxide
+ thioredoxin
      Cofactor: Selenium; Zinc
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     oxidoreductase activity     4 terms  

 

 
    reference    
 
 
DOI no: 10.1107/S0907444908028060 Acta Crystallogr D Biol Crystallogr 64:1116-1122 (2008)
PubMed id: 19020349  
 
 
The plug-based nanovolume Microcapillary Protein Crystallization System (MPCS).
C.J.Gerdts, M.Elliott, S.Lovell, M.B.Mixon, A.J.Napuli, B.L.Staker, P.Nollert, L.Stewart.
 
  ABSTRACT  
 
The Microcapillary Protein Crystallization System (MPCS) embodies a new semi-automated plug-based crystallization technology which enables nanolitre-volume screening of crystallization conditions in a plasticware format that allows crystals to be easily removed for traditional cryoprotection and X-ray diffraction data collection. Protein crystals grown in these plastic devices can be directly subjected to in situ X-ray diffraction studies. The MPCS integrates the formulation of crystallization cocktails with the preparation of the crystallization experiments. Within microfluidic Teflon tubing or the microfluidic circuitry of a plastic CrystalCard, approximately 10-20 nl volume droplets are generated, each representing a microbatch-style crystallization experiment with a different chemical composition. The entire protein sample is utilized in crystallization experiments. Sparse-matrix screening and chemical gradient screening can be combined in one comprehensive ;hybrid' crystallization trial. The technology lends itself well to optimization by high-granularity gradient screening using optimization reagents such as precipitation agents, ligands or cryoprotectants.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 MPCS components. (a) A picture of the components of the MPCS system. (b) Screenshots of the operational modes of the MicroPlugger software. (c) A picture of the MPCS CrystalCard filled with dyed protein crystals. (d) A picture of the PDMS/Teflon CrystalCard typically used for the hybrid method.
Figure 5.
Figure 5 Methionine-R-sulfoxide reductase. (a) A microphotograph of a methionine-R-sulfoxide reductase crystal. (b) F[o] - F[c] OMIT map contoured at 3 for Cys residues and a Zn ion. (c) Ribbon diagram of the NCS dimer of methionine-R-sulfoxide reductase from Burkholderia pseudomallei. Zinc ions are represented as gold spheres and acetate ions in ball-and-stick representation. The structure was deposited as PDB entry 3cxk .
 
  The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallogr D Biol Crystallogr (2008, 64, 1116-1122) copyright 2008.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20000709 L.Li, W.Du, and R.F.Ismagilov (2010).
Multiparameter screening on SlipChip used for nanoliter protein crystallization combining free interface diffusion and microbatch methods.
  J Am Chem Soc, 132, 112-119.
PDB code: 3kjr
20810277 M.Chruszcz, M.Domagalski, T.Osinski, A.Wlodawer, and W.Minor (2010).
Unmet challenges of structural genomics.
  Curr Opin Struct Biol, 20, 587-597.  
19929835 C.L.Verlinde, E.Fan, S.Shibata, Z.Zhang, Z.Sun, W.Deng, J.Ross, J.Kim, L.Xiao, T.L.Arakaki, J.Bosch, J.M.Caruthers, E.T.Larson, I.Letrong, A.Napuli, A.Kelly, N.Mueller, F.Zucker, W.C.Van Voorhis, E.A.Merritt, and W.G.Hol (2009).
Fragment-based cocktail crystallography by the medical structural genomics of pathogenic protozoa consortium.
  Curr Top Med Chem, 9, 1678-1687.  
19594426 P.J.Myler, R.Stacy, L.Stewart, B.L.Staker, W.C.Van Voorhis, G.Varani, and G.W.Buchko (2009).
The Seattle Structural Genomics Center for Infectious Disease (SSGCID).
  Infect Disord Drug Targets, 9, 493-506.  
19855826 W.C.Van Voorhis, W.G.Hol, P.J.Myler, and L.J.Stewart (2009).
The role of medical structural genomics in discovering new drugs for infectious diseases.
  PLoS Comput Biol, 5, e1000530.  
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.