2X5P

Crystal structure of the Streptococcus pyogenes fibronectin binding protein Fbab-B

Summary for 2X5P

• Entry DOI: 10.2210/pdb2x5p/pdb
• Descriptor: FIBRONECTIN BINDING PROTEIN (2 entities in total)
• Functional Keywords: protein binding
• Biological source: STREPTOCOCCUS PYOGENES
• Total number of polymer chains: 1
• Total formula weight: 12883.23

Authors

Oke, M.,Carter, L.G.,Johnson, K.A.,Liu, H.,Mcmahon, S.A.,White, M.F.,Naismith, J.H. (deposition date: 2010-02-10, release date: 2010-09-01, Last modification date: 2024-05-08)

Primary citation

Oke, M.,Carter, L.G.,Johnson, K.A.,Liu, H.,Mcmahon, S.A.,Yan, X.,Kerou, M.,Weikart, N.D.,Kadi, N.,Sheikh, M.A.,Schmelz, S.,Dorward, M.,Zawadzki, M.,Cozens, C.,Falconer, H.,Powers, H.,Overton, I.M.,Van Niekerk, C.A.J.,Peng, X.,Patel, P.,Garrett, R.A.,Prangishvili, D.,Botting, C.H.,Coote, P.J.,Dryden, D.T.F.,Barton, G.J.,Schwarz-Linek, U.,Challis, G.L.,Taylor, G.L.,White, M.F.,Naismith, J.H.
The Scottish Structural Proteomics Facility: Targets, Methods and Outputs.
J.Struct.Funct.Genomics, 11:167-, 2010

PubMed Abstract: The Scottish Structural Proteomics Facility was funded to develop a laboratory scale approach to high throughput structure determination. The effort was successful in that over 40 structures were determined. These structures and the methods harnessed to obtain them are reported here. This report reflects on the value of automation but also on the continued requirement for a high degree of scientific and technical expertise. The efficiency of the process poses challenges to the current paradigm of structural analysis and publication. In the 5 year period we published ten peer-reviewed papers reporting structural data arising from the pipeline. Nevertheless, the number of structures solved exceeded our ability to analyse and publish each new finding. By reporting the experimental details and depositing the structures we hope to maximize the impact of the project by allowing others to follow up the relevant biology.

PubMed: 20419351
DOI: 10.1007/S10969-010-9090-Y

Experimental method

X-RAY DIFFRACTION (1.6 Å)