1pei | pdb_00001pei

NMR STRUCTURE OF THE MEMBRANE-BINDING DOMAIN OF CTP PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE, 10 STRUCTURES

spinqualitylabelsall models 1pei, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pei is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: ACE, NH2 Activity: Choline-phosphate cytidylyltransferase, with EC number 2.7.7.15 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PCY1A_RAT] Controls phosphatidylcholine synthesis. Publication Abstract from PubMed It has been proposed that the domain of the regulatory enzyme, CTP:phosphocholine cytidylyltransferase, which mediates reversible binding of the enzyme to membranes, is an amphipathic alpha-helix of approximately 60 amino acid residues and that this domain is adjacent to the putative active site domain of this enzyme. Circular dichroism indicated that the secondary structures of two overlapping peptides spanning this region were predominantly alpha-helical in the presence of PG vesicles or sodium dodecyl sulfate micelles. Interproton distances were obtained from two-dimensional NMR spectroscopic measurements to solve the structures of these two peptides. The C-terminal 22 amino acid peptide segment (corresponding to Val267-Ser288) was a well-defined alpha-helix over its length. The N-terminal 33-mer (corresponding to Asn236-Glu268) was composed of an alpha-helix from Glu243 to Lys266, a well-structured bend of about 50 degrees at Tyr240-His241-Leu242, and an N-terminal four-residue helix. It is proposed that the three residues involved in generating the bend act as the hinge between the catalytic and regulatory domains. The nonpolar faces of the 33-mer and 22-mer were interrupted by Ser260, Ser271, and Ser282. These residues may serve to limit the hydrophobicity and facilitate reversible and lipid-selective membrane binding. The hydrophobic faces of the helices were flanked by a set of basic amino acid residues on one side and basic amino acid residues interspersed with glutamates on the other. The disposition of these side chains gives clues to the basis for the specificities of these peptides for anionic surfaces. Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase.,Dunne SJ, Cornell RB, Johnson JE, Glover NR, Tracey AS Biochemistry. 1996 Sep 17;35(37):11975-84. PMID:8810902 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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