1mqs
Crystal structure of Sly1p in complex with an N-terminal peptide of Sed5pCrystal structure of Sly1p in complex with an N-terminal peptide of Sed5p
Structural highlights
FunctionSLY1_YEAST Able to suppress the functional loss of YPT1. SLY1 is essential for cell viability. May interact indirectly, or directly with YPT1. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCytosolic Sec1/munc18-like proteins (SM proteins) are recruited to membrane fusion sites by interaction with syntaxin-type SNARE proteins, constituting indispensable positive regulators of intracellular membrane fusion. Here we present the crystal structure of the yeast SM protein Sly1p in complex with a short N-terminal peptide derived from the Golgi-resident syntaxin Sed5p. Sly1p folds, similarly to neuronal Sec1, into a three-domain arch-shaped assembly, and Sed5p interacts in a helical conformation predominantly with domain I of Sly1p on the opposite site of the nSec1/syntaxin-1-binding site. Sequence conservation of the major interactions suggests that homologues of Sly1p as well as the paralogous Vps45p group bind their respective syntaxins in the same way. Furthermore, we present indirect evidence that nSec1 might be able to contact syntaxin 1 in a similar fashion. The observed Sly1p-Sed5p interaction mode therefore indicates how SM proteins can stay associated with the assembling fusion machinery in order to participate in late fusion steps. Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p.,Bracher A, Weissenhorn W EMBO J. 2002 Nov 15;21(22):6114-24. PMID:12426383[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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