Does anyone know the oligomeric state of the mature and functional lipoprotein lipL32 in Leptospira?
It's an outer membrane-bound protein. In its mature state, the signal peptide (residues 1-20) is removed, and the cysteine (resid 21) reacts and binds with the head group of a lipid. I've looked through many articles, from x-ray to western blots, and although I understand its structure in terms of the single protein, the results from the x-ray crystal data (as per the protein data bank) are my cause for confusion.
These are the results from LipL32 in the PDB. Three different structures, a multi-mer, and two different dimers.
Are these different geometries the result of the experiment, or is the protein's quaternary structure as one would expect in the organism?