1jjh

E2 DNA-binding Domain from Bovine Papillomavirus Type 1E2 DNA-binding Domain from Bovine Papillomavirus Type 1

Structural highlights 1jjh is a 3 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1by9, 2bop, 1f9f, 1jj4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [VE2_BPV1] E2 regulates viral transcription and DNA replication. Binds to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory region. Can either activate or repress transcription depending on E2RE's position with regards to proximal promoter elements. Repression occurs by sterically hindering the assembly of the transcription initiation complex. The E1-E2 complex binds to the origin of DNA replication. 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 2.5 A crystal structures of the DNA-binding domain of the E2 protein from bovine papillomavirus strain 1 and its complex with DNA are presented. E2 is a transcriptional regulatory protein that is also involved in viral DNA replication. It is the structural prototype for a novel class of DNA-binding proteins: dimeric beta-barrels with surface alpha-helices that serve as recognition helices. These helices contain the amino-acid residues involved in sequence-specifying interactions. The E2 proteins from different papillomavirus strains recognize and bind to the same consensus 12 base-pair DNA sequence. However, recent evidence from solution studies points to differences in the mechanisms by which E2 from the related viral strains bovine papillomavirus-1 and human papillomavirus-16 discriminate between DNA targets based on non-contacted nucleotide sequences. This report provides evidence that sequence-specific DNA-binding is accompanied by a rearrangement of protein subunits and deformation of the DNA. These results suggest that, along with DNA sequence-dependent conformational properties, protein subunit orientation plays a significant role in the mechanisms of target selection utilized by E2. Subunit rearrangement accompanies sequence-specific DNA binding by the bovine papillomavirus-1 E2 protein.,Hegde RS, Wang AF, Kim SS, Schapira M J Mol Biol. 1998 Mar 6;276(4):797-808. PMID:9500927 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Regulatory protein E2

spinqualitylabelsall models 1jjh, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image