1a44
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1a44" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a44, resolution 1.84Å" /> '''PHOSPHATIDYLETHANOLA...)
Next diff →
Revision as of 08:28, 20 November 2007
|
PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN FROM CALF BRAIN
Overview
BACKGROUND: Phosphatidylethanolamine-binding protein (PEBP) is a basic, protein found in numerous tissues from a wide range of species. The, screening of gene and protein data banks defines a family of PEBP-related, proteins that are present in a variety of organisms, including Drosophila, and inferior eukaryotes. PEBP binds to phosphatidylethanolamine and, nucleotides in vitro, but its biological function in vivo is not yet, known. The expression of PEBP and related proteins seems to be correlated, with development and cell morphogenesis, however. To obtain new insights, into the PEBP family and its potential functions, we initiated a, crystallographic study of bovine brain PEPB. RESULTS: The X-ray crystal, structure of bovine brain PEBP has been solved using multiple isomorphous, replacement methods, and refined to 1.84 A resolution. The structure, displays a beta fold and exhibits one nonprolyl cis peptide bond. Analysis, of cavities within the structure and sequence alignments were used to, identify a putative ligand-binding site. This binding site is defined by, residues of the C-terminal helix and the residues His85, Asp69, Gly109 and, Tyr119. This site also corresponds to the binding site of, phosphorylethanolamine, the polar head group of phosphatidylethanolamine., CONCLUSIONS: This study shows that PEBP is not related to the G-protein, family nor to known lipid-binding proteins, and therefore defines a novel, structural family of phospholipid-binding proteins. The PEBP structure, contains no internal hydrophobic pocket, as described for lipocalins or, small phospholipid-transfer proteins. Nevertheless, in PEBP, a small, cavity close to the protein surface has a high affinity for anions, such, as phosphate and acetate, and also phosphorylethanolamine. We suggest that, this cavity corresponds to the binding site of the polar head group of, phosphatidylethanolamine.
About this Structure
1A44 is a Single protein structure of sequence from Bos taurus with ACT as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the phosphatidylethanolamine-binding protein from bovine brain: a novel structural class of phospholipid-binding proteins., Serre L, Vallee B, Bureaud N, Schoentgen F, Zelwer C, Structure. 1998 Oct 15;6(10):1255-65. PMID:9782057
Page seeded by OCA on Tue Nov 20 10:35:52 2007
