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PDBsum entry 4yyc

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protein ligands metals links
Transferase PDB id
4yyc

 

 

 

 

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Contents
Protein chain
479 a.a.
Ligands
UNL
Metals
_CL
Waters ×530
PDB id:
4yyc
Name: Transferase
Title: Crystal structure of trimethylamine methyltransferase from sinorhizobium meliloti in complex with unknown ligand
Structure: Putative trimethylamine methyltransferase. Chain: a. Engineered: yes
Source: Rhizobium meliloti. Ensifer meliloti. Organism_taxid: 266834. Strain: 1021. Gene: mttb, r01976, smc04330. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
1.56Å     R-factor:   0.140     R-free:   0.165
Authors: I.G.Shabalin,P.J.Porebski,O.A.Gasiorowska,K.B.Handing, E.Niedzialkowska,M.T.Cymborowski,D.R.Cooper,M.Stead,J.Hammonds, M.Ahmed,J.Bonanno,R.Seidel,S.C.Almo,W.Minor,New York Structural Genomics Research Consortium (Nysgrc)
Key ref: E.Niedzialkowska et al. (2016). Protein purification and crystallization artifacts: The tale usually not told. Protein Sci, 25, 720-733. PubMed id: 26660914 DOI: 10.1002/pro.2861
Date:
23-Mar-15     Release date:   08-Apr-15    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q92P20  (Q92P20_RHIME) -  Methyltransferase from Rhizobium meliloti (strain 1021)
Seq:
Struc:
 
Seq:
Struc:
524 a.a.
479 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.1.1.-  - ?????
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1002/pro.2861 Protein Sci 25:720-733 (2016)
PubMed id: 26660914  
 
 
Protein purification and crystallization artifacts: The tale usually not told.
E.Niedzialkowska, O.Gasiorowska, K.B.Handing, K.A.Majorek, P.J.Porebski, I.G.Shabalin, E.Zasadzinska, M.Cymborowski, W.Minor.
 
  ABSTRACT  
 
The misidentification of a protein sample, or contamination of a sample with the wrong protein, may be a potential reason for the non-reproducibility of experiments. This problem may occur in the process of heterologous overexpression and purification of recombinant proteins, as well as purification of proteins from natural sources. If the contaminated or misidentified sample is used for crystallization, in many cases the problem may not be detected until structures are determined. In the case of functional studies, the problem may not be detected for years. Here several procedures that can be successfully used for the identification of crystallized protein contaminants, including: (i) a lattice parameter search against known structures, (ii) sequence or fold identification from partially built models, and (iii) molecular replacement with common contaminants as search templates have been presented. A list of common contaminant structures to be used as alternative search models was provided. These methods were used to identify four cases of purification and crystallization artifacts. This report provides troubleshooting pointers for researchers facing difficulties in phasing or model building.
 

 

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