1x9x
From Proteopedia
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'''Solution Structure of Dimeric SAM Domain from MAPKKK Ste11''' | '''Solution Structure of Dimeric SAM Domain from MAPKKK Ste11''' | ||
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[[Category: Wu, C.]] | [[Category: Wu, C.]] | ||
[[Category: Xu, P.]] | [[Category: Xu, P.]] | ||
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| - | [[Category: | + | [[Category: Sam domain]] |
| - | [[Category: | + | [[Category: Ste11]] |
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Revision as of 11:45, 3 May 2008
Solution Structure of Dimeric SAM Domain from MAPKKK Ste11
Overview
Ste11, a homologue of mammalian MAPKKKs, together with its binding partner Ste50 works in a number of MAPK signaling pathways of Saccharomyces cerevisiae. Ste11/Ste50 binding is mediated by their sterile alpha motifs or SAM domains, of which homologues are also found in many other intracellular signaling and regulatory proteins. Here, we present the solution structure of the SAM domain or residues D37-R104 of Ste11 and its interactions with the cognate SAM domain-containing region of Ste50, residues M27-Q131. NMR pulse-field-gradient (PFG) and rotational correlation time measurements (tauc) establish that the Ste11 SAM domain exists predominantly as a symmetric dimer in solution. The solution structure of the dimeric Ste11 SAM domain consists of five well-defined helices per monomer packed into a compact globular structure. The dimeric structure of the SAM domain is maintained by a novel dimer interface involving interactions between a number of hydrophobic residues situated on helix 4 and at the beginning of the C-terminal long helix (helix 5). The dimer structure may also be stabilized by potential salt bridge interactions across the interface. NMR H/2H exchange experiments showed that binding of the Ste50 SAM to the Ste11 SAM very likely involves the positively charged extreme C-terminal region as well as exposed hydrophobic patches of the dimeric Ste11 SAM domain. The dimeric structure of the Ste11 SAM and its interactions with the Ste50 SAM may have important roles in the regulation and activation of the Ste11 kinase and signal transmission and amplifications through the Ste50-Ste11 complex.
About this Structure
1X9X is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex., Bhattacharjya S, Xu P, Gingras R, Shaykhutdinov R, Wu C, Whiteway M, Ni F, J Mol Biol. 2004 Dec 3;344(4):1071-87. PMID:15544813 Page seeded by OCA on Sat May 3 14:45:39 2008
