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==NMR STRUCTURE OF THE MEMBRANE-BINDING DOMAIN OF CTP PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE, 10 STRUCTURES==
<StructureSection load='1pei' size='340' side='right'caption='[[1pei]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pei]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PEI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PEI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pei OCA], [https://pdbe.org/1pei PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pei RCSB], [https://www.ebi.ac.uk/pdbsum/1pei PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pei ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PCY1A_RAT PCY1A_RAT] Controls phosphatidylcholine synthesis.
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== 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<ref>PMID:8810902</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Cornell RB]]
[[Category: Dunne SJ]]
[[Category: Glover NR]]
[[Category: Johnson JE]]
[[Category: Tracey AS]]