1dhm
From Proteopedia
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'''DNA-BINDING DOMAIN OF E2 FROM HUMAN PAPILLOMAVIRUS-31, NMR, MINIMIZED AVERAGE STRUCTURE''' | '''DNA-BINDING DOMAIN OF E2 FROM HUMAN PAPILLOMAVIRUS-31, NMR, MINIMIZED AVERAGE STRUCTURE''' | ||
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[[Category: Walter, K.]] | [[Category: Walter, K.]] | ||
[[Category: Yoon, H S.]] | [[Category: Yoon, H S.]] | ||
| - | [[Category: | + | [[Category: Dna-binding protein]] |
| - | [[Category: | + | [[Category: Early protein]] |
| - | [[Category: | + | [[Category: Trans-acting factor]] |
| - | [[Category: | + | [[Category: Transcriptional activator]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:51:23 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:51, 2 May 2008
DNA-BINDING DOMAIN OF E2 FROM HUMAN PAPILLOMAVIRUS-31, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
The three-dimensional structure of the DNA-binding domain of the E2 protein from human papillomavirus-31 was determined by using multidimensional heteronuclear nuclear magnetic resonance (NMR) spectroscopy. A total of 1429 NMR-derived distance and dihedral angle restraints were obtained for each of the 83-residue subunits of this symmetric dimer. The average root mean square deviations of 20 structures calculated using a distance geometry-simulated annealing protocol are 0.59 and 0.90 angstroms for the backbone and all heavy atoms, respectively, for residues 2-83. The structure of the human virus protein free in solution consists of an eight-stranded beta-barrel and two pairs of alpha-helices. Although the overall fold of the protein is similar to the crystal structure of the bovine papillomavirus-1 E2 protein when complexed to DNA, several small but interesting differences were observed between these two structures at the subunit interface. In addition, a beta-hairpin that contacts DNA in the crystal structure of the protein-DNA complex is disordered in the NMR structures, and steady-state 1H-15N heteronuclear NOE measurements indicate that this region is highly mobile in the absence of DNA. The recognition helix also appears to be flexible, as evidenced by fast amide exchange rates. This phenomenon has also been observed for a number of other DNA-binding proteins and may constitute a common theme in protein/DNA recognition.
About this Structure
1DHM is a Single protein structure of sequence from Human papillomavirus. Full crystallographic information is available from OCA.
Reference
Solution structure of the DNA-binding domain of a human papillomavirus E2 protein: evidence for flexible DNA-binding regions., Liang H, Petros AM, Meadows RP, Yoon HS, Egan DA, Walter K, Holzman TF, Robins T, Fesik SW, Biochemistry. 1996 Feb 20;35(7):2095-103. PMID:8652551 Page seeded by OCA on Fri May 2 13:51:23 2008
