5ed4 | pdb_00005ed4

Structure of a PhoP-DNA complex

spinqualitylabelsall models 5ed4, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ed4 is a 8 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CAC, EDO Gene: phoP, ABI38_13965, AC434_12840, BN1303_02986, ERS024750_01197, ERS024751_02016, ERS024758_01633, ERS124824_03492, ERS124825_03677, ERS124827_03481, ERS124828_03492, ERS124829_03387, ERS124830_03452, ERS124831_03570, ERS124832_03594, IQ38_16185, IQ42_15805, IQ45_15620, IQ47_15575, IQ48_15690, IU13_15815, IU15_16135, IU16_15745, IU17_15635, IU21_16005, T209_15560 ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) Activity: Alkaline phosphatase, with EC number 3.1.3.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The transcriptional regulator PhoP is an essential virulence factor in Mycobacterium tuberculosis, and it presents a target for the development of new anti-tuberculosis drugs and attenuated tuberculosis vaccine strains. PhoP binds to DNA as a highly cooperative dimer by recognizing direct repeats of 7-bp motifs with a 4-bp spacer. To elucidate the PhoP-DNA binding mechanism, we determined the crystal structure of the PhoP-DNA complex. The structure revealed a tandem PhoP dimer that bound to the direct repeat. The surprising tandem arrangement of the receiver domains allowed the four domains of the PhoP dimer to form a compact structure, accounting for the strict requirement of a 4-bp spacer and the highly cooperative binding of the dimer. The PhoP-DNA interactions exclusively involved the effector domain. The sequence-recognition helix made contact with the bases of the 7-bp motif in the major groove, and the wing interacted with the adjacent minor groove. The structure provides a starting point for the elucidation of the mechanism by which PhoP regulates the virulence of M. tuberculosis and guides the design of screening platforms for PhoP inhibitors. Structural basis of DNA sequence recognition by the response regulator PhoP in Mycobacterium tuberculosis.,He X, Wang L, Wang S Sci Rep. 2016 Apr 15;6:24442. doi: 10.1038/srep24442. PMID:27079268 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Response regulator 3D structure

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