3AL1
DESIGNED PEPTIDE ALPHA-1, RACEMIC P1BAR FORM
Summary for 3AL1
Entry DOI | 10.2210/pdb3al1/pdb |
Descriptor | PROTEIN (D, L-ALPHA-1), (4S)-2-METHYL-2,4-PENTANEDIOL, ETHANOLAMINE, ... (4 entities in total) |
Functional Keywords | helical bilayer, biomaterial, centric, racemic, structural protein |
Total number of polymer chains | 2 |
Total formula weight | 3123.89 |
Authors | Patterson, W.R.,Anderson, D.H.,Degrado, W.F.,Cascio, D.,Eisenberg, D. (deposition date: 1998-10-26, release date: 1998-11-04, Last modification date: 2024-10-30) |
Primary citation | Patterson, W.R.,Anderson, D.H.,DeGrado, W.F.,Cascio, D.,Eisenberg, D. Centrosymmetric bilayers in the 0.75 A resolution structure of a designed alpha-helical peptide, D,L-Alpha-1. Protein Sci., 8:1410-1422, 1999 Cited by PubMed Abstract: We report the 0.75 A crystal structure of a racemic mixture of the 12-residue designed peptide "Alpha-1" (Acetyl-ELLKKLLEELKG), the L-enantiomer of which is described in the accompanying paper. Equivalent solutions of the centrosymmetric bilayers were determined by two direct phasing programs in space groups P1 and P1bar. The unit cell contains two L-alpha-helices and two D-alpha-helices. The columnar-sheet bilayer motif seen in L-Alpha-1 is maintained in the D,L-Alpha-1 structure except that each sheet of head-to-tail helices is composed of one enantiomer and is related to its neighboring sheets by inversion symmetry. Comparison to the L-Alpha-1 structure provides further insight into peptide design. The high resolution and small asymmetric unit allowed building an intricate model (R = 13.1%, Rfree = 14.5%) that incorporates much of the discrete disorder of peptide and solvent. Ethanolamine and 2-methyl-2,4-pentanediol (MPD) molecules bind near helix termini. Rigid body analysis identifies sites of restricted displacements and torsions. Side-chain discrete disorder propagates into the backbone of one helix but not the other. Although no side chain in Alpha-1 is rigid, the environments in the crystal restrict some of them to no or only one active torsion. PubMed: 10422829PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (0.75 Å) |
Structure validation
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