2hsg

Structure of transcription regulator CcpA in its DNA-free stateStructure of transcription regulator CcpA in its DNA-free state

Structural highlights 2hsg is a 1 chain structure with sequence from Priestia megaterium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CCPA_PRIMG Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The catabolite control protein A (CcpA) from Bacillus megaterium is a member of the bacterial repressor protein family GalR-LacI. CcpA functions as master transcriptional regulator of carbon catabolite repression/regulation in firmicutes. Here we present the crystal structure of full-length apo CcpA at 2.5 A resolution from B. megaterium. The structure reveals the location of the helix-turn-helix domain as well as the hinge region, which were not visible due to their high flexibility in earlier crystallographic studies on CcpA molecules. The structure of the apo CcpA homodimer in the present form is in contrast to other reported structures for CcpA. Structure of full-length transcription regulator CcpA in the apo form.,Loll B, Saenger W, Biesiadka J Biochim Biophys Acta. 2007 Jun;1774(6):732-6. Epub 2007 Apr 18. PMID:17500051 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Catabolite control protein 3D structures

spinqualitylabelsall models 2hsg, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image