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From Proteopedia
Mad structure of the periplasmique domain of the Escherichia coli PAL protein
Structural highlights
FunctionPAL_ECOLI Thought to play a role in bacterial envelope integrity. Very strongly associated with the peptidoglycan. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli.,Abergel C, Walburger A, Chenivesse S, Lazdunski C Acta Crystallogr D Biol Crystallogr. 2001 Feb;57(Pt 2):317-9. PMID:11173492[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. Loading citation details.. Citations No citations found See AlsoReferences
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