Protein Family Models

This is leucine-zipper is found in the enterobacterial outer membrane lipoprotein LPP. It is likely that this domain oligomerises and is involved in protein-protein interactions. As such it is a bundle of alpha-helical coiled-coils, which are known to play key roles in mediating specific protein-protein interactions for in molecular recognition and the assembly of multi-protein complexes. [1]. 10843861. Core structure of the outer membrane lipoprotein from Escherichia coli at 1.9 A resolution. Shu W, Liu J, Ji H, Lu M;. J Mol Biol. 2000;299:1101-1112. [2]. 12054830. Core side-chain packing and backbone conformation in Lpp-56 coiled-coil mutants. Liu J, Cao W, Lu M;. J Mol Biol. 2002;318:877-888. [3]. 12741822. Zinc-mediated helix capping in a triple-helical protein. Liu J, Dai J, Lu M;. Biochemistry. 2003;42:5657-5664. [4]. 15520380. Atomic structure of a tryptophan-zipper pentamer. Liu J, Yong W, Deng Y, Kallenbach NR, Lu M;. Proc Natl Acad Sci U S A. 2004;101:16156-16161. [5]. 16828114. Conformational transition between four and five-stranded phenylalanine zippers determined by a local packing interaction. Liu J, Zheng Q, Deng Y, Kallenbach NR, Lu M;. J Mol Biol. 2006;361:168-179. (from Pfam)

Date:

2024-10-16

This model derives from PF11839 but is more narrowly focused. All member sequences of the seed alignment are bacterial lipoproteins between 78 and 103 amino acids in length. Members include OprI (major outer membrane lipoprotein I) from Pseudomonas aeruginosa, and Lpp (Braun’s lipoprotein), called the most abundant protein in Escherichia coli. Lpp becomes covalently linked to the cell wall, while anchored in the inner leaflet of the outer membrane, providing structural stability to the cell envelope.

Date:

2021-11-10