1rr7
From Proteopedia
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|PDB= 1rr7 |SIZE=350|CAPTION= <scene name='initialview01'>1rr7</scene>, resolution 2.2Å | |PDB= 1rr7 |SIZE=350|CAPTION= <scene name='initialview01'>1rr7</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=PT:PLATINUM (II) ION'>PT</scene> | + | |LIGAND= <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= Mor ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 Enterobacteria phage Mu]) | |GENE= Mor ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 Enterobacteria phage Mu]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rr7 OCA], [http://www.ebi.ac.uk/pdbsum/1rr7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rr7 RCSB]</span> | ||
}} | }} | ||
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[[Category: Kumaraswami, M.]] | [[Category: Kumaraswami, M.]] | ||
[[Category: Park, H W.]] | [[Category: Park, H W.]] | ||
| - | [[Category: PT]] | ||
[[Category: mor]] | [[Category: mor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:31:53 2008'' |
Revision as of 20:31, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | Mor (Enterobacteria phage Mu) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the Middle Operon Regulator protein of Bacteriophage Mu
Overview
Transcription from the middle promoter, Pm, of bacteriophage Mu requires the phage-encoded activator protein Mor and bacterial RNA polymerase. Mor is a sequence-specific DNA-binding protein that mediates transcription activation through its interactions with the C-terminal domains of the alpha and sigma subunits of bacterial RNA polymerase. Here we present the first structure for a member of the Mor/C family of transcription activators, the crystal structure of Mor to 2.2-A resolution. Each monomer of the Mor dimer is composed of two domains, the N-terminal dimerization domain and C-terminal DNA-binding domain, which are connected by a linker containing a beta strand. The N-terminal dimerization domain has an unusual mode of dimerization; helices alpha1 and alpha2 of both monomers are intertwined to form a four-helix bundle, generating a hydrophobic core that is further stabilized by antiparallel interactions between the two beta strands. Mutational analysis of key leucine residues in helix alpha1 demonstrated a role for this hydrophobic core in protein solubility and function. The C-terminal domain has a classical helix-turn-helix DNA-binding motif that is located at opposite ends of the elongated dimer. Since the distance between the two helix-turn-helix motifs is too great to allow binding to two adjacent major grooves of the 16-bp Mor-binding site, we propose that conformational changes in the protein and DNA will be required for Mor to interact with the DNA. The highly conserved glycines flanking the beta strand may act as pivot points, facilitating the conformational changes of Mor, and the DNA may be bent.
About this Structure
1RR7 is a Single protein structure of sequence from Enterobacteria phage mu. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Mor protein of bacteriophage Mu, a member of the Mor/C family of transcription activators., Kumaraswami M, Howe MM, Park HW, J Biol Chem. 2004 Apr 16;279(16):16581-90. Epub 2004 Jan 16. PMID:14729670
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