Figure 1. Listeria adhesion protein (LAP) structure predicted from homology modeling (ModBase).

(A) LAP is an alcohol acetaldehyde dehydrogenase enzyme (AAD; 866 aa) and consists of an N-terminal acetaldehyde dehydrogenase (ALDH) and a C-terminal alcohol dehydrogenase region (ADH). The ALDH and ADH domains are modeled separately. The C terminus also contains an iron binding domain. (B) LAP is composed of alpha helices, beta sheets, and loop structures. N-terminal ALDH was determined to be composed of 3 independent subdomains: N1 (Met₁–Pro₂₂₃), N2 (Gly₂₂₄–Gly₄₁₁), and N3 (Gly₄₁₂–Pro₄₆₄). Similarly, C-terminal ADH was defined as having 2 independent subdomains: C1 (Pro₄₆₅–Val₆₄₈) and C2 (Pro₆₄₉–Val₈₆₆). N3 is a loop region that connects the LAP N- and C-terminus and is thought to be incapable of independent Hsp60 interaction; hence, this region was cloned and expressed in conjunction with the C1 subdomain. The N1, N2, N3, C1, and C2 subdomains are colored in blue, yellow, white, green, and red, respectively. Also using the same color scheme, the bottom panel represents the full LAP sequence and partitioned into the colored subdomains (boxed and labeled by the ending amino acid positions for each subdomain).