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PDBsum entry 2o31

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protein ligands links
Signaling protein PDB id
2o31
Jmol
Contents
Protein chain
67 a.a. *
Ligands
FMT ×2
Waters ×101
* Residue conservation analysis
PDB id:
2o31
Name: Signaling protein
Title: Crystal structure of the second sh3 domain from ponsin
Structure: Ponsin. Chain: a. Fragment: src homology 3 (sh3) domain. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: sorbs1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Resolution:
1.50Å     R-factor:   0.132     R-free:   0.162
Authors: N.Pinotsis,M.Wilmanns,I.Margiolaki
Key ref: I.Margiolaki et al. (2007). Second SH3 domain of ponsin solved from powder diffraction. J Am Chem Soc, 129, 11865-11871. PubMed id: 17784760 DOI: 10.1021/ja073846c
Date:
30-Nov-06     Release date:   23-Oct-07    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9BX66  (SRBS1_HUMAN) -  Sorbin and SH3 domain-containing protein 1
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
1292 a.a.
67 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     actin filament organization   2 terms 

 

 
DOI no: 10.1021/ja073846c J Am Chem Soc 129:11865-11871 (2007)
PubMed id: 17784760  
 
 
Second SH3 domain of ponsin solved from powder diffraction.
I.Margiolaki, J.P.Wright, M.Wilmanns, A.N.Fitch, N.Pinotsis.
 
  ABSTRACT  
 
Determination of protein crystal structures is dependent on the growth of high-quality single crystals, a process that is not always successful. Optimum crystallization conditions must be systematically sought for, and microcrystalline powders are frequently obtained in failed attempts to grow the desired crystal. In materials science, structures of samples ranging from ceramics, pharmaceuticals, zeolites, etc., can nowadays be solved, almost routinely, from powdered samples, and there seems to be no fundamental reason, except the sheer size and complexity of the structures involved, why powder diffraction should not be employed to solve structures of small proteins. Indeed, recent work has shown that the high-quality powder diffraction data can be used in the study of protein crystal structures. We report the solution, model building, and refinement of a 67-residue protein domain crystal structure, with a cell volume of 64 879 A3, from powder diffraction. The second SH3 domain of ponsin, a protein of high biological significance due to its role in cellular processes, is determined and refined to resolution limits comparable to single-crystal techniques. Our results demonstrate the power and future applicability of the powder technique in structural biology.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21382498 K.Fujii, M.T.Young, and K.D.Harris (2011).
Exploiting powder X-ray diffraction for direct structure determination in structural biology: The P2X4 receptor trafficking motif YEQGL.
  J Struct Biol, 174, 461-467.  
21154412 R.A.Dilanian, C.Darmanin, J.N.Varghese, S.W.Wilkins, T.Oka, N.Yagi, H.M.Quiney, and K.A.Nugent (2011).
A new approach for structure analysis of two-dimensional membrane protein crystals using X-ray powder diffraction data.
  Protein Sci, 20, 457-464.  
20606255 S.Basso, C.Besnard, J.P.Wright, I.Margiolaki, A.Fitch, P.Pattison, and M.Schiltz (2010).
Features of the secondary structure of a protein molecule from powder diffraction data.
  Acta Crystallogr D Biol Crystallogr, 66, 756-761.  
19307716 J.A.Doebbler, and R.B.Von Dreele (2009).
Application of molecular replacement to protein powder data from image plates.
  Acta Crystallogr D Biol Crystallogr, 65, 348-355.  
18156682 I.Margiolaki, and J.P.Wright (2008).
Powder crystallography on macromolecules.
  Acta Crystallogr A, 64, 169-180.  
18156673 W.I.David, and K.Shankland (2008).
Structure determination from powder diffraction data.
  Acta Crystallogr A, 64, 52-64.  
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.