1r63

<StructureSection load='1r63' size='340' side='right'caption='[[1r63]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1r63]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bp434 Bp434]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R63 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R63 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=1r63 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r63 OCA], [https://pdbe.org/1r63 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r63 RCSB], [https://www.ebi.ac.uk/pdbsum/1r63 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r63 ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/RPC1_BP434 RPC1_BP434]] Binds to two sets of three contiguous operator sites in the phage genome.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The independently folding 63-residue N-terminal DNA-binding domain of the 434 repressor, 434(1-63), contains a buried Arg10-Glu35 salt bridge. A corresponding salt bridge is found in a variety of prokaryotic and eukaryotic DNA-binding proteins with helix-turn-helix motifs. Here, the NMR solution structures of 434(1-63) and the mutant protein 434[R10M](1-63) were determined to investigate the structural role of this salt bridge. Both proteins contain the same type of global fold, with five alpha-helices and a helix-turn-helix motif formed by the helices II and III. The primary structural difference caused by the Arg10 --&gt; Met mutation is a translation of helix I along its axis relative to the helix II-turn-helix III motif. This limited conformational change is paralleled by a 9 kJ M(-1) decrease of the stability of the folded mutant protein in aqueous solution at pH 4.8. It affects the pKa value of Glu19 as well as the population of a hydrogen bond between the backbone amide proton of Asn16 and the side-chain carboxylate group of Glu19. Using the crystal structure of the 434 repressor dimer complexed with the operator DNA as a basis, model building of the DNA complex with the NMR structure of 434[R10M](1-63) shows that Asn16, which is located on the protein surface, makes direct contact with the DNA and indicates that the point mutation Arg10 --&gt; Met should also lead to modifications of the protein-protein contacts in the complex.

Structural role of a buried salt bridge in the 434 repressor DNA-binding domain.,Pervushin K, Billeter M, Siegal G, Wuthrich K J Mol Biol. 1996 Dec 20;264(5):1002-12. PMID:9000626<ref>PMID:9000626</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1r63" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bp434]]

[[Category: Billeter, M]]

[[Category: Pervushin, K V]]

[[Category: Siegal, G]]

[[Category: Wuthrich, K]]

[[Category: Phage 434 repressor]]