1z1v: Difference between revisions
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==NMR structure of the Saccharomyces cerevisiae Ste50 SAM domain== | ==NMR structure of the Saccharomyces cerevisiae Ste50 SAM domain== | ||
<StructureSection load='1z1v' size='340' side='right' caption='[[1z1v | <StructureSection load='1z1v' size='340' side='right'caption='[[1z1v]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1z1v]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1z1v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z1V FirstGlance]. <br> | ||
</td></tr><tr id=' | </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=1z1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z1v OCA], [https://pdbe.org/1z1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z1v RCSB], [https://www.ebi.ac.uk/pdbsum/1z1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z1v ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/STE50_YEAST STE50_YEAST] Involved in growth arrest during conjugation. May interact with the G protein alpha subunit. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 23: | Line 22: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Donaldson | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Kwan | [[Category: Donaldson LW]] | ||
[[Category: Maini | [[Category: Kwan JJ]] | ||
[[Category: Pawson | [[Category: Maini J]] | ||
[[Category: Warner | [[Category: Pawson T]] | ||
[[Category: Warner N]] | |||
Latest revision as of 12:31, 6 December 2023
NMR structure of the Saccharomyces cerevisiae Ste50 SAM domainNMR structure of the Saccharomyces cerevisiae Ste50 SAM domain
Structural highlights
FunctionSTE50_YEAST Involved in growth arrest during conjugation. May interact with the G protein alpha subunit. Publication Abstract from PubMedIn Saccharomyces cerevisiae, signal transduction through pathways governing mating, osmoregulation, and nitrogen starvation depends upon a direct interaction between the sterile alpha motif (SAM) domains of the Ste11 mitogen-activated protein kinase kinase kinase (MAPKKK) and its regulator Ste50. Previously, we solved the NMR structure of the SAM domain from Ste11 and identified two mutants that diminished binding to the Ste50 SAM domain. Building upon the Ste11 study, we present the NMR structure of the monomeric Ste50 SAM domain and a series of mutants bearing substitutions at surface-exposed hydrophobic amino acid residues. The mid-loop (ML) region of Ste11-SAM, defined by helices H3 and H4 and the end-helix (EH) region of Ste50-SAM, defined by helix H5, were sensitive to substitution, indicating that these two surfaces contribute to the high-affinity interaction. The combination of two mutants, Ste11-SAM-L72R and Ste50-SAM-L69R, formed a high-affinity heterodimer unencumbered by competing homotypic interactions that had prevented earlier NMR studies of the wild-type complex. Yeast bearing mutations that prevented the heterotypic Ste11-Ste50 association in vitro presented signaling defects in the mating and high-osmolarity growth pathways. Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction.,Kwan JJ, Warner N, Maini J, Chan Tung KW, Zakaria H, Pawson T, Donaldson LW J Mol Biol. 2006 Feb 10;356(1):142-54. Epub 2005 Nov 28. PMID:16337230[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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