1OAP

Mad structure of the periplasmique domain of the Escherichia coli PAL protein

1OAP の概要

• エントリーDOI: 10.2210/pdb1oap/pdb
• 分子名称: PEPTIDOGLYCAN-ASSOCIATED LIPOPROTEIN, SULFATE ION (3 entities in total)
• 機能のキーワード: periplasmic, peptidoglycan binding, tol system, outer membrane, lipoprotein
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12507.87

構造登録者

Abergel, C.,Walburger, A.,Bouveret, E.,Claverie, J.M. (登録日: 2003-01-20, 公開日: 2004-02-13, 最終更新日: 2024-05-08)

主引用文献

Abergel, C.,Walburger, A.,Chenivesse, S.,Lazdunski, C.
Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli.
Acta Crystallogr.,Sect.D, 57:317-319, 2001

PubMed Abstract: The peptidoglycan-associated lipoprotein (Pal) from Escherichia coli is part of the Tol--Pal multiprotein complex used by group A colicins to penetrate and kill cells. Pal homologues are found in many Gram-negative bacteria and the Tol--Pal system is thought to play a role in bacterial envelope integrity. The Pal protein comprises 152 amino acids. Crystals of the C-terminal 109-amino-acid fragment of the Pal protein have been produced. The crystals belong to the tetragonal space group I4(1), with unit-cell parameters a = b = 89.3, c = 67.2 A. There are two molecules in the asymmetric unit. Frozen crystals diffract to at least 2.8 A resolution using synchrotron radiation. Selenomethionine-substituted truncated Pal protein is currently being produced in order to use multiwavelength anomalous dispersion (MAD) for phasing.

PubMed: 11173492
DOI: 10.1107/s0907444900019739

実験手法

X-RAY DIFFRACTION (1.93 Å)