1MQS

Crystal structure of Sly1p in complex with an N-terminal peptide of Sed5p

Summary for 1MQS

• Entry DOI: 10.2210/pdb1mqs/pdb
• Related: 1DN1 1EPU 1FVF 1FVH
• Descriptor: Sly1 Protein, Integral Membrane Protein SED5 (3 entities in total)
• Functional Keywords: sm-protein, snare, syntaxin, endocytosis-exocytosis complex, endocytosis/exocytosis
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm: P22213; Membrane ; Single-pass type IV membrane protein : Q01590
• Total number of polymer chains: 2
• Total formula weight: 81605.25

Authors

Bracher, A.,Weissenhorn, W. (deposition date: 2002-09-17, release date: 2002-11-20, Last modification date: 2024-10-30)

Primary citation

Bracher, A.,Weissenhorn, W.
Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p
Embo J., 21:6114-6124, 2002

PubMed Abstract: Cytosolic 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.

PubMed: 12426383
DOI: 10.1093/emboj/cdf608

Experimental method

X-RAY DIFFRACTION (3 Å)