PDBsum entry 1oap

Lipoprotein

PDB id

1oap

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Contents

			Protein chain

					108 a.a. *

			Ligands

					SO4 ×2

			Waters ×86

* Residue conservation analysis

PDB id:

1oap

Links

Name:

Lipoprotein

Title:

Mad structure of the periplasmique domain of the escherichia coli pal protein

Structure:

Peptidoglycan-associated lipoprotein. Chain: a. Fragment: periplasmic domain, residues 65-137. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Other_details: periplasmic domain

Resolution:

1.93Å

R-factor:

0.200

R-free:

0.234

Authors:

C.Abergel,A.Walburger,E.Bouveret,J.M.Claverie

Key ref:

C.Abergel et al. (2001). Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli. Acta Crystallogr D Biol Crystallogr, 57, 317-319. PubMed id: 11173492

Date:

20-Jan-03

Release date:

13-Feb-04

PROCHECK

	Headers

	References

Protein chain

P0A912 (PAL_ECOLI) - Peptidoglycan-associated lipoprotein from Escherichia coli (strain K12)

Seq: Struc:					173 a.a. 108 a.a.

Key:

Secondary structure

CATH domain

	Acta Crystallogr D Biol Crystallogr 57:317-319 (2001)
PubMed id: 11173492

Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli.
C.Abergel, A.Walburger, S.Chenivesse, C.Lazdunski.

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.