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1KQ4

CRYSTAL STRUCTURE OF A THY1-COMPLEMENTING PROTEIN (TM0449) FROM THERMOTOGA MARITIMA AT 2.25 A RESOLUTION

Summary for 1KQ4
Entry DOI10.2210/pdb1kq4/pdb
Related1KQ3
DescriptorHYPOTHETICAL PROTEIN TM0449, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
Functional Keywordsthy1-complementing protein, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi, transferase
Biological sourceThermotoga maritima
Total number of polymer chains4
Total formula weight114282.40
Authors
Wilson, I.A.,Miller, M.D.,Joint Center for Structural Genomics (JCSG) (deposition date: 2002-01-03, release date: 2002-02-27, Last modification date: 2024-11-20)
Primary citationLesley, S.A.,Kuhn, P.,Godzik, A.,Deacon, A.M.,Mathews, I.,Kreusch, A.,Spraggon, G.,Klock, H.E.,McMullan, D.,Shin, T.,Vincent, J.,Robb, A.,Brinen, L.S.,Miller, M.D.,McPhillips, T.M.,Miller, M.A.,Scheibe, D.,Canaves, J.M.,Guda, C.,Jaroszewski, L.,Selby, T.L.,Elsliger, M.-A.,Wooley, J.,Taylor, S.S.,Hodgson, K.O.,Wilson, I.A.,Schultz, P.G.,Stevens, R.C.
Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline
Proc.Natl.Acad.Sci.USA, 99:11664-11669, 2002
Cited by
PubMed Abstract: Structural genomics is emerging as a principal approach to define protein structure-function relationships. To apply this approach on a genomic scale, novel methods and technologies must be developed to determine large numbers of structures. We describe the design and implementation of a high-throughput structural genomics pipeline and its application to the proteome of the thermophilic bacterium Thermotoga maritima. By using this pipeline, we successfully cloned and attempted expression of 1,376 of the predicted 1,877 genes (73%) and have identified crystallization conditions for 432 proteins, comprising 23% of the T. maritima proteome. Representative structures from TM0423 glycerol dehydrogenase and TM0449 thymidylate synthase-complementing protein are presented as examples of final outputs from the pipeline.
PubMed: 12193646
DOI: 10.1073/pnas.142413399
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.25 Å)
Structure validation

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