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2X0O

Apo structure of the Alcaligin biosynthesis protein C (AlcC) from Bordetella bronchiseptica

Summary for 2X0O
Entry DOI10.2210/pdb2x0o/pdb
Related2X0P 2X0Q
DescriptorALCALIGIN BIOSYNTHESIS PROTEIN, SULFATE ION (3 entities in total)
Functional Keywordsbiosynthetic protein, alcaligin biosynthesis, adenylation, siderophores, iron acquisition
Biological sourceBORDETELLA BRONCHISEPTICA
Total number of polymer chains1
Total formula weight70528.31
Authors
Johnson, K.A.,Schmelz, S.,Kadi, N.,Mcmahon, S.A.,Oke, M.,Liu, H.,Carter, L.G.,White, M.F.,Challis, G.L.,Naismith, J.H. (deposition date: 2009-12-16, release date: 2010-07-28, Last modification date: 2023-12-20)
Primary citationOke, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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