1al1
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1al1 |SIZE=350|CAPTION= <scene name='initialview01'>1al1</scene>, resolution 2.7Å | |PDB= 1al1 |SIZE=350|CAPTION= <scene name='initialview01'>1al1</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1al1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1al1 OCA], [http://www.ebi.ac.uk/pdbsum/1al1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1al1 RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Hill, C P.]] | [[Category: Hill, C P.]] | ||
[[Category: Wesson, L.]] | [[Category: Wesson, L.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: SO4]] | ||
[[Category: synthetic protein model]] | [[Category: synthetic protein model]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:42:29 2008'' |
Revision as of 15:42, 30 March 2008
| |||||||
| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF ALPHA1: IMPLICATIONS FOR PROTEIN DESIGN
Overview
X-ray diffraction shows the structure of a synthetic protein model, formed from noncovalent self-association of a 12-residue peptide and of sulfate ions at low pH. This peptide is a fragment of a 16-residue polypeptide that was designed to form an amphiphilic alpha helix with a ridge of Leu residues along one helical face. By interdigitation of the leucines of four such helices, the design called for self-association into a four-alpha-helical bundle. The crystal structure (2.7 angstrom resolution; R factor = 0.215) reveals a structure more complex than the design, with both a tetramer and a hexamer. The alpha-helical tetramer with leucine interior has more oblique crossing angles than most four-alpha-helical bundles; the hexamer has a globular hydrophobic core of 12 leucine residues and three associated sulfate ions. Computational analysis suggests that the hexameric association is tighter than the tetrameric one. The consistency of the structure with the design is discussed, as well as the divergence.
About this Structure
1AL1 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Crystal structure of alpha 1: implications for protein design., Hill CP, Anderson DH, Wesson L, DeGrado WF, Eisenberg D, Science. 1990 Aug 3;249(4968):543-6. PMID:2382133
Page seeded by OCA on Sun Mar 30 18:42:29 2008
