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1peh

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(New page: 200px<br /><applet load="1peh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1peh" /> '''NMR STRUCTURE OF THE MEMBRANE-BINDING DOMAIN...)
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[[Image:1peh.jpg|left|200px]]<br /><applet load="1peh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1peh" />
 
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'''NMR STRUCTURE OF THE MEMBRANE-BINDING DOMAIN OF CTP PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE, 10 STRUCTURES'''<br />
 
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==Overview==
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==NMR STRUCTURE OF THE MEMBRANE-BINDING DOMAIN OF CTP PHOSPHOCHOLINE CYTIDYLYLTRANSFERASE, 10 STRUCTURES==
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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.
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<StructureSection load='1peh' size='340' side='right'caption='[[1peh]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1peh]] 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=1PEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PEH FirstGlance]. <br>
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1PEH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with ACE and NH2 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Choline-phosphate_cytidylyltransferase Choline-phosphate cytidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.15 2.7.7.15] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PEH OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1peh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1peh OCA], [https://pdbe.org/1peh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1peh RCSB], [https://www.ebi.ac.uk/pdbsum/1peh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1peh ProSAT]</span></td></tr>
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8810902 8810902]
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</table>
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[[Category: Choline-phosphate cytidylyltransferase]]
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== Function ==
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[https://www.uniprot.org/uniprot/PCY1A_RAT PCY1A_RAT] Controls phosphatidylcholine synthesis.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/1peh_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1peh ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Cornell RB]]
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[[Category: Cornell, R.B.]]
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[[Category: Dunne SJ]]
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[[Category: Dunne, S.J.]]
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[[Category: Glover NR]]
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[[Category: Glover, N.R.]]
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[[Category: Johnson JE]]
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[[Category: Johnson, J.E.]]
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[[Category: Tracey AS]]
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[[Category: Tracey, A.S.]]
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[[Category: ACE]]
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[[Category: NH2]]
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[[Category: membrane]]
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[[Category: nucleotidyltransferase]]
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[[Category: phospholipid biosynthesis]]
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[[Category: phosphorylation]]
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[[Category: repeat]]
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[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:44:24 2007''
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Current revision

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

PDB ID 1peh

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