|
|
| (5 intermediate revisions not shown.) |
| Line 1: |
Line 1: |
| | + | |
| | ==DESIGNED TRIMERIC COILED COIL-VALD== | | ==DESIGNED TRIMERIC COILED COIL-VALD== |
| - | <StructureSection load='1coi' size='340' side='right' caption='[[1coi]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='1coi' size='340' side='right'caption='[[1coi]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1coi]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1COI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1coi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1COI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COI FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1coi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1coi OCA], [http://pdbe.org/1coi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1coi RCSB], [http://www.ebi.ac.uk/pdbsum/1coi PDBsum]</span></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=1coi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1coi OCA], [https://pdbe.org/1coi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1coi RCSB], [https://www.ebi.ac.uk/pdbsum/1coi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1coi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 20: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Synthetic construct sequences]] | + | [[Category: Large Structures]] |
| - | [[Category: Degrado, W F]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Eisenberg, D]] | + | [[Category: Degrado WF]] |
| - | [[Category: Ogihara, N L]] | + | [[Category: Eisenberg D]] |
| - | [[Category: Weiss, M S]] | + | [[Category: Ogihara NL]] |
| - | [[Category: Alpha-helical bundle]]
| + | [[Category: Weiss MS]] |
| - | [[Category: Coiled coil design]]
| + | |
| - | [[Category: Protein design]]
| + | |
| Structural highlights
Publication Abstract from PubMed
The three-dimensional structure of the 29-residue designed coiled coil having the amino acid sequence acetyl-E VEALEKK VAALESK VQALEKK VEALEHG-amide has been determined and refined to a crystallographic R-factor of 21.4% for all data from 10-A to 2.1-A resolution. This molecule is called coil-VaLd because it contains valine in the a heptad positions and leucine in the d heptad positions. In the trigonal crystal, three molecules, related by a crystallographic threefold axis, form a parallel three-helix bundle. The bundles are stacked head-to-tail to form a continuous coiled coil along the c-direction of the crystal. The contacts among the three helices within the coiled coil are mainly hydrophobic: four layers of valine residues alternate with four layers of leucine residues to form the core of the bundle. In contrast, mostly hydrophilic contacts mediate the interaction between trimers: here a total of two direct protein--protein hydrogen bonds are found. Based on the structure, we propose a scheme for designing crystals of peptides containing continuous two-, three-, and four-stranded coiled coils.
The crystal structure of the designed trimeric coiled coil coil-VaLd: implications for engineering crystals and supramolecular assemblies.,Ogihara NL, Weiss MS, Degrado WF, Eisenberg D Protein Sci. 1997 Jan;6(1):80-8. PMID:9007979[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ogihara NL, Weiss MS, Degrado WF, Eisenberg D. The crystal structure of the designed trimeric coiled coil coil-VaLd: implications for engineering crystals and supramolecular assemblies. Protein Sci. 1997 Jan;6(1):80-8. PMID:9007979
|
