4A5K

Structural analyses of Slm1-PH domain demonstrate ligand binding in the non-canonical site

Summary for 4A5K

• Entry DOI: 10.2210/pdb4a5k/pdb
• Related: 4A6F 4A6H 4A6K
• Descriptor: PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE-BINDING PROTEIN SLM 1, SULFATE ION (3 entities in total)
• Functional Keywords: signaling protein, non-canonical binding site, inositol phosphate, phosphoserine
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST)
• Cellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side: P40485
• Total number of polymer chains: 4
• Total formula weight: 54289.65

Authors

Anand, K.,Gavin, A.C. (deposition date: 2011-10-25, release date: 2012-06-13, Last modification date: 2023-12-20)

Primary citation

Anand, K.,Maeda, K.,Gavin, A.C.
Structural Analyses of Slm1-Ph Domain Demonstrate Ligand Binding in the Non-Canonical Site
Plos One, 7:36526-, 2012

PubMed Abstract: Pleckstrin homology (PH) domains are common membrane-targeting modules and their best characterized ligands are a set of important signaling lipids that include phosphatidylinositol phosphates (PtdInsPs). PH domains recognize PtdInsPs through two distinct mechanisms that use different binding pockets on opposite sides of the β-strands 1 and 2: i) a canonical binding site delimited by the β1-β2 and β3-β4loops and ii) a non-canonical binding site bordered by the β1-β2 and β5-β6loops. The PH domain-containing protein Slm1 from budding yeast Saccharomyces cerevisiae is required for actin cytoskeleton polarization and cell growth. We recently reported that this PH domain binds PtdInsPs and phosphorylated sphingolipids in a cooperative manner.

PubMed: 22574179
DOI: 10.1371/JOURNAL.PONE.0036526

Experimental method

X-RAY DIFFRACTION (1.76 Å)