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[[Image:1rr7.gif|left|200px]]


{{Structure
==Crystal structure of the Middle Operon Regulator protein of Bacteriophage Mu==
|PDB= 1rr7 |SIZE=350|CAPTION= <scene name='initialview01'>1rr7</scene>, resolution 2.2&Aring;
<StructureSection load='1rr7' size='340' side='right'caption='[[1rr7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=PT:PLATINUM (II) ION'>PT</scene>
<table><tr><td colspan='2'>[[1rr7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Mu Escherichia virus Mu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RR7 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
|GENE= Mor ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10677 Enterobacteria phage Mu])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rr7 OCA], [https://pdbe.org/1rr7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rr7 RCSB], [https://www.ebi.ac.uk/pdbsum/1rr7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rr7 ProSAT]</span></td></tr>
 
</table>
'''Crystal structure of the Middle Operon Regulator protein of Bacteriophage Mu'''
== Function ==
 
[https://www.uniprot.org/uniprot/MOR_BPMU MOR_BPMU] Activator of the Pm promoter, which controls middle genes expression. Activation of Pm allows expression of protein C necessary for late gene expression. In addition to Mor binding, activation of Pm might require the interaction of Mor with the C-terminus of host RNAP subunits RpoA and RpoH.<ref>PMID:2173258</ref> <ref>PMID:8790343</ref>
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/rr/1rr7_consurf.spt"</scriptWhenChecked>
1RR7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RR7 OCA].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
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:[http://www.ncbi.nlm.nih.gov/pubmed/14729670 14729670]
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1rr7 ConSurf].
[[Category: Enterobacteria phage mu]]
<div style="clear:both"></div>
[[Category: Single protein]]
== References ==
[[Category: Howe, M M.]]
<references/>
[[Category: Kumaraswami, M.]]
__TOC__
[[Category: Park, H W.]]
</StructureSection>
[[Category: PT]]
[[Category: Escherichia virus Mu]]
[[Category: mor]]
[[Category: Large Structures]]
 
[[Category: Howe MM]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:55:11 2008''
[[Category: Kumaraswami M]]
[[Category: Park HW]]

Latest revision as of 08:25, 14 February 2024

Crystal structure of the Middle Operon Regulator protein of Bacteriophage Mu

1rr7, resolution 2.20Å

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