1OAP

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

Summary for 1OAP

• Entry DOI: 10.2210/pdb1oap/pdb
• Descriptor: PEPTIDOGLYCAN-ASSOCIATED LIPOPROTEIN, SULFATE ION (3 entities in total)
• Functional Keywords: periplasmic, peptidoglycan binding, tol system, outer membrane, lipoprotein
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 12507.87

Authors

Abergel, C.,Walburger, A.,Bouveret, E.,Claverie, J.M. (deposition date: 2003-01-20, release date: 2004-02-13, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.93 Å)