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==DETERMINATION OF THE NUCLEAR MAGNETIC RESONANCE STRUCTURE OF THE DNA-BINDING DOMAIN OF THE P22 C2 REPRESSOR (1-76) IN SOLUTION AND COMPARISON WITH THE DNA-BINDING DOMAIN OF THE 434 REPRESSOR==
==DETERMINATION OF THE NUCLEAR MAGNETIC RESONANCE STRUCTURE OF THE DNA-BINDING DOMAIN OF THE P22 C2 REPRESSOR (1-76) IN SOLUTION AND COMPARISON WITH THE DNA-BINDING DOMAIN OF THE 434 REPRESSOR==
<StructureSection load='1adr' size='340' side='right'caption='[[1adr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='1adr' size='340' side='right'caption='[[1adr]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1adr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpp22 Bpp22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ADR FirstGlance]. <br>
<table><tr><td colspan='2'>[[1adr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_virus_P22 Salmonella virus P22]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ADR FirstGlance]. <br>
</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=1adr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adr OCA], [https://pdbe.org/1adr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1adr RCSB], [https://www.ebi.ac.uk/pdbsum/1adr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1adr ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1adr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adr OCA], [https://pdbe.org/1adr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1adr RCSB], [https://www.ebi.ac.uk/pdbsum/1adr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1adr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/RPC2_BPP22 RPC2_BPP22]] This protein allows the phage to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein C2 to the OR and OL operators, preventing transcription of proteins necessary for lytic development.  
[https://www.uniprot.org/uniprot/RPC2_BPP22 RPC2_BPP22] This protein allows the phage to reside inactively in the chromosome of its host bacterium. This lysogenic state is maintained by binding of regulatory protein C2 to the OR and OL operators, preventing transcription of proteins necessary for lytic development.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1adr ConSurf].
</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=1adr ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The solution structure of the N-terminal DNA-binding domain of the P22 c2 repressor (residues 1 to 76) was determined by nuclear magnetic resonance (NMR) spectroscopy. The structure determination was based on nearly complete sequence-specific resonance assignments for 1H, 13C and 15N, and tables of the chemical shifts for all three nuclei are included here. A group of 20 conformers was calculated from the NMR constraints using the program DIANA, and energy-minimized using an implementation of the AMBER force field in the program OPAL. The core of the protein formed by residues 5 to 68 is structurally well defined, with an average of 0.7 A for the root-mean-square deviations calculated for the backbone atoms of the individual conformers relative to the mean coordinates. The N-terminal tetrapeptide segment and the C-terminal octapeptide segment are flexibly disordered. The molecular architecture includes five alpha-helical segments with residues 6 to 17, 21 to 28, 32 to 39, 47 to 57 and 61 to 65. The length and relative orientation of these helices are closely similar to the arrangement of corresponding regular secondary structures in the DNA-binding domain of the 434 repressor, with the sole exception of the fourth helix, which is one turn longer at its amino-terminal end than the corresponding helix in the 434 repressor. This extension of the fourth helix implies that the DNA-binding mode of the P22 c2 repressor must be somewhat different from that observed for the 434 repressor. Exact superposition of two P22 c2 repressor DNA-binding domains for best fit of corresponding polypeptide backbone atoms onto the two 434 repressor DNA-binding domains in the crystal structure of the 434 repressor-DNA complex would result in a model of the P22 c2 repressor-DNA complex which could not accommodate the fourth helices because of steric overlap.
Determination of the nuclear magnetic resonance structure of the DNA-binding domain of the P22 c2 repressor (1 to 76) in solution and comparison with the DNA-binding domain of the 434 repressor.,Sevilla-Sierra P, Otting G, Wuthrich K J Mol Biol. 1994 Jan 21;235(3):1003-20. PMID:8289306<ref>PMID:8289306</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1adr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpp22]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Otting, G]]
[[Category: Salmonella virus P22]]
[[Category: Sevillasierra, P]]
[[Category: Otting G]]
[[Category: Wuthrich, K]]
[[Category: Sevillasierra P]]
[[Category: Transcription regulation]]
[[Category: Wuthrich K]]

Revision as of 15:23, 13 March 2024

DETERMINATION OF THE NUCLEAR MAGNETIC RESONANCE STRUCTURE OF THE DNA-BINDING DOMAIN OF THE P22 C2 REPRESSOR (1-76) IN SOLUTION AND COMPARISON WITH THE DNA-BINDING DOMAIN OF THE 434 REPRESSOR

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