1j0r: Difference between revisions
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< | ==Crystal structure of the replication termination protein mutant C110S== | ||
<StructureSection load='1j0r' size='340' side='right'caption='[[1j0r]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
or the | <table><tr><td colspan='2'>[[1j0r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J0R FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</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=1j0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j0r OCA], [https://pdbe.org/1j0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j0r RCSB], [https://www.ebi.ac.uk/pdbsum/1j0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j0r ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RTP_BACSU RTP_BACSU] Plays a role in DNA replication and termination (fork arrest mechanism). Two dimers of rtp bind to the two inverted repeat regions (IRI and IRII) present in the termination site. The binding of each dimer is centered on an 8 bp direct repeat. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We report the structural and biophysical consequences of cysteine substitutions in the DNA-binding replication terminator protein (RTP) of Bacillus subtilis, that resulted in an optimised RTP mutant suitable for structural studies. The cysteine residue 110 was replaced with alanine, valine or serine. Protein secondary structure and stability (using circular dichroism spectropolarimetry), self-association (using analytical ultracentrifugation), and DNA-binding measurements revealed RTP.C110S to be the most similar mutant to wild-type RTP. The C110A and C110V.RTP mutants were less soluble, less stable and showed lower DNA-binding affinity. The structure of RTP.C110S, solved to 2.5A resolution using crystallographic methods, showed no major structural perturbation due to the mutation. Heteronuclear NMR spectroscopic studies revealed subtle differences in the electronic environment about the site of mutation. The study demonstrates the suitability of serine as a substitute for cysteine in RTP and the high sensitivity of protein behaviour to single amino acid substitutions. | |||
The impact of single cysteine residue mutations on the replication terminator protein.,Vivian JP, Hastings AF, Duggin IG, Wake RG, Wilce MC, Wilce JA Biochem Biophys Res Commun. 2003 Oct 31;310(4):1096-103. PMID:14559228<ref>PMID:14559228</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1j0r" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Replication Termination Protein|Replication Termination Protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Duggin | [[Category: Duggin IG]] | ||
[[Category: Hastings | [[Category: Hastings AF]] | ||
[[Category: Vivian | [[Category: Vivian JP]] | ||
[[Category: Wake | [[Category: Wake RG]] | ||
[[Category: Wilce | [[Category: Wilce JA]] | ||
[[Category: Wilce | [[Category: Wilce MCJ]] | ||
Latest revision as of 13:28, 16 August 2023
Crystal structure of the replication termination protein mutant C110SCrystal structure of the replication termination protein mutant C110S
Structural highlights
FunctionRTP_BACSU Plays a role in DNA replication and termination (fork arrest mechanism). Two dimers of rtp bind to the two inverted repeat regions (IRI and IRII) present in the termination site. The binding of each dimer is centered on an 8 bp direct repeat. Publication Abstract from PubMedWe report the structural and biophysical consequences of cysteine substitutions in the DNA-binding replication terminator protein (RTP) of Bacillus subtilis, that resulted in an optimised RTP mutant suitable for structural studies. The cysteine residue 110 was replaced with alanine, valine or serine. Protein secondary structure and stability (using circular dichroism spectropolarimetry), self-association (using analytical ultracentrifugation), and DNA-binding measurements revealed RTP.C110S to be the most similar mutant to wild-type RTP. The C110A and C110V.RTP mutants were less soluble, less stable and showed lower DNA-binding affinity. The structure of RTP.C110S, solved to 2.5A resolution using crystallographic methods, showed no major structural perturbation due to the mutation. Heteronuclear NMR spectroscopic studies revealed subtle differences in the electronic environment about the site of mutation. The study demonstrates the suitability of serine as a substitute for cysteine in RTP and the high sensitivity of protein behaviour to single amino acid substitutions. The impact of single cysteine residue mutations on the replication terminator protein.,Vivian JP, Hastings AF, Duggin IG, Wake RG, Wilce MC, Wilce JA Biochem Biophys Res Commun. 2003 Oct 31;310(4):1096-103. PMID:14559228[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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