1a44: Difference between revisions

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New page: left|200px<br /><applet load="1a44" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a44, resolution 1.84Å" /> '''PHOSPHATIDYLETHANOLA...
 
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[[Image:1a44.gif|left|200px]]<br /><applet load="1a44" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1a44.gif|left|200px]]<br /><applet load="1a44" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1a44, resolution 1.84&Aring;" />
caption="1a44, resolution 1.84&Aring;" />
'''PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN FROM CALF BRAIN'''<br />
'''PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN FROM CALF BRAIN'''<br />


==Overview==
==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.
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==
==About this Structure==
1A44 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A44 OCA].  
1A44 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A44 OCA].  


==Reference==
==Reference==
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[[Category: lipid-binding]]
[[Category: lipid-binding]]


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