1QSU

CRYSTAL STRUCTURE OF THE TRIPLE-HELICAL COLLAGEN-LIKE PEPTIDE, (PRO-HYP-GLY)4-GLU-LYS-GLY(PRO-HYP-GLY)5

1QSU の概要

• エントリーDOI: 10.2210/pdb1qsu/pdb
• 分子名称: PROTEIN ((PRO-HYP-GLY)4- GLU-LYS-GLY(PRO-HYP-GLY)5) (2 entities in total)
• 機能のキーワード: triple helix, structural protein
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 8216.68

構造登録者

Kramer, R.Z.,Venugopal, M.,Bella, J.,Brodsky, B.,Berman, H.M. (登録日: 1999-06-23, 公開日: 2000-08-30, 最終更新日: 2025-03-26)

主引用文献

Kramer, R.Z.,Venugopal, M.G.,Bella, J.,Mayville, P.,Brodsky, B.,Berman, H.M.
Staggered molecular packing in crystals of a collagen-like peptide with a single charged pair.
J.Mol.Biol., 301:1191-1205, 2000

PubMed Abstract: The crystal structure of the triple-helical peptide, (Pro-Hyp-Gly)(4)-Glu-Lys-Gly-(Pro-Hyp-Gly)(5) has been determined to 1.75 A resolution. This peptide was designed to examine the effect of a pair of adjacent, oppositely charged residues on collagen triple-helical conformation and intermolecular interactions. The molecular conformation (a 7(5) triple helix) and hydrogen bonding schemes are similar to those previously reported for collagen triple helices and provides a second instance of water mediated N--H . . . O==C interchain hydrogen bonds for the amide group of the residue following Gly. Although stereochemically capable of forming intramolecular or intermolecular ion pairs, the lysine and glutamic acid side-chains instead display direct interactions with carbonyl groups and hydroxyproline hydroxyl groups or interactions mediated by water molecules. Solution studies on the EKG peptide indicate stabilization at neutral pH values, where both Glu and Lys are ionized, but suggest that this occurs because of the effects of ionization on the individual residues, rather than ion pair formation. The EKG structure suggests a molecular mechanism for such stabilization through indirect hydrogen bonding. The molecular packing in the crystal includes an axial stagger between molecules, reminiscent of that observed in D-periodic collagen fibrils. The presence of a Glu-Lys-Gly triplet in the middle of the sequence appears to mediate this staggered molecular packing through its indirect water-mediated interactions with backbone C==O groups and side chains.

PubMed: 10966815
DOI: 10.1006/jmbi.2000.4017

実験手法

X-RAY DIFFRACTION (1.75 Å)