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1p9i

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(New page: 200px<br /><applet load="1p9i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p9i, resolution 1.17&Aring;" /> '''Coiled-coil X-ray st...)
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[[Image:1p9i.jpg|left|200px]]<br /><applet load="1p9i" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1p9i, resolution 1.17&Aring;" />
 
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'''Coiled-coil X-ray structure at 1.17 A resolution'''<br />
 
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==Overview==
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==Coiled-coil X-ray structure at 1.17 A resolution==
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We determined the 1.17 A resolution X-ray crystal structure of a hybrid, peptide based on sequences from coiled-coil regions of the proteins GCN4, and cortexillin I. The peptide forms a parallel homodimeric coiled-coil, with C(alpha) backbone geometry similar to GCN4 (rmsd value 0.71 A). Three, stabilizing interactions have been identified: a unique hydrogen, bonding-electrostatic network not previously observed in coiled-coils, and, two other hydrophobic interactions involving leucine residues at positions, e and g from both g-a' and d-e' interchain interactions with the, hydrophobic core. This is also the first report of the quantitative, significance of these interactions. The GCN4/cortexillin hybrid, surprisingly has two interchain Glu-Lys' ion pairs that form a hydrogen, bonding network with the Asn residues in the core. This network, which was, not observed for the reversed Lys-Glu' pair in GCN4, increases the, combined stability contribution of each Glu-Lys' salt bridge across the, central Asn15-Asn15' core to approximately 0.7 kcal/mole, compared to, approximately 0.4 kcal mole(-1) from a Glu-Lys' salt bridge on its own. In, addition to electrostatic and hydrogen bonding stabilization of the, coiled-coil, individual leucine residues at positions e and g in the, hybrid peptide also contribute to stability by 0.7 kcal/mole relative to, alanine. These interactions are of critical importance to understanding, the stability requirements for coiled-coil folding and in modulating the, stability of de novo designed macromolecules containing this motif.
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<StructureSection load='1p9i' size='340' side='right'caption='[[1p9i]], [[Resolution|resolution]] 1.17&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1p9i]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P9I FirstGlance]. <br>
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1P9I is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P9I OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.17&#8491;</td></tr>
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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=1p9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9i OCA], [https://pdbe.org/1p9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p9i RCSB], [https://www.ebi.ac.uk/pdbsum/1p9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p9i ProSAT]</span></td></tr>
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==Reference==
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</table>
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Unique stabilizing interactions identified in the two-stranded alpha-helical coiled-coil: crystal structure of a cortexillin I/GCN4 hybrid coiled-coil peptide., Lee DL, Ivaninskii S, Burkhard P, Hodges RS, Protein Sci. 2003 Jul;12(7):1395-405. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12824486 12824486]
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__TOC__
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[[Category: Protein complex]]
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</StructureSection>
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[[Category: Ivaninskii, S.]]
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[[Category: Large Structures]]
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[[Category: coiled-coil]]
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[[Category: Ivaninskii S]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:13:52 2007''
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Current revision

Coiled-coil X-ray structure at 1.17 A resolution

PDB ID 1p9i

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