1LEN

REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION

1LEN の概要

• エントリーDOI: 10.2210/pdb1len/pdb
• 分子名称: LECTIN, PHOSPHATE ION, MANGANESE (II) ION, ... (6 entities in total)
• 機能のキーワード: lectin
• 由来する生物種: Lens culinaris (lentil); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 51622.51

構造登録者

Van Overberge, D.,Loris, R.,Wyns, L. (登録日: 1993-11-17, 公開日: 1994-01-31, 最終更新日: 2024-02-14)

主引用文献

Loris, R.,Van Overberge, D.,Dao-Thi, M.H.,Poortmans, F.,Maene, N.,Wyns, L.
Structural analysis of two crystal forms of lentil lectin at 1.8 A resolution.
Proteins, 20:330-346, 1994

PubMed Abstract: The structures of two crystal forms of lentil lectin are determined and refined at high resolution. Orthorhombic lentil lectin is refined at 1.80 A resolution to an R-factor of 0.184 and monoclinic lentil lectin at 1.75 A resolution to an R-factor of 0.175. These two structures are compared to each other and to the other available legume lectin structures. The monosaccharide binding pocket of each lectin monomer contains a tightly bound phosphate ion. This phosphate makes hydrogen bonding contacts with Asp-81 beta, Gly-99 beta, and Asn-125 beta, three residues that are highly conserved in most of the known legume lectin sequences and essential for monosaccharide recognition in all legume lectin crystal structures described thus far. A detailed analysis of the composition and properties of the hydrophobic contact network and hydrophobic nuclei in lentil lectin is presented. Contact map calculations reveal that dense clusters of nonpolar as well as polar side chains play a major role in secondary structure packing. This is illustrated by a large cluster of 24 mainly hydrophobic amino acids that is responsible for the majority of packing interactions between the two beta-sheets. Another series of four smaller and less hydrophobic clusters is found to mediate the packing of a number of loop structures upon the front sheet. A very dense, but not very conserved cluster is found to stabilize the transition metal binding site. The highly conserved and invariant nonpolar residues are distributed asymmetrically over the protein.

PubMed: 7731952
DOI: 10.1002/prot.340200406

実験手法

X-RAY DIFFRACTION (1.8 Å)