Alpha-lytic protease

Alpha-lytic protease (ALP) is a bacterial serine protease of the chymotrypsin family. ALP is a two-domain enzyme. One domain is a large pro region (residues 1-199) that catalyzes the folding of the protease. The second domain is the protease domain (residues 200-397).^[1]

. Water molecules are shown as red spheres.
(PDB entry 3pro).^[2]

3D Structures of alpha-lytic protease

Alpha-lytic protease 3D structures

Structure of alpha-lytic protease protease domain (green) and pro domain (magenta) complex with benzenesulfonyl fluoride (PDB entry 3pro)

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ReferencesReferences

↑ Bone R, Frank D, Kettner CA, Agard DA. Structural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates. Biochemistry. 1989 Sep 19;28(19):7600-9. PMID:2611204
↑ Sauter NK, Mau T, Rader SD, Agard DA. Structure of alpha-lytic protease complexed with its pro region. Nat Struct Biol. 1998 Nov;5(11):945-50. PMID:9808037 doi:http://dx.doi.org/10.1038/2919

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Michal Harel, Alexander Berchansky

[1] Bone R, Frank D, Kettner CA, Agard DA. Structural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates. Biochemistry. 1989 Sep 19;28(19):7600-9. PMID:2611204

[2] Sauter NK, Mau T, Rader SD, Agard DA. Structure of alpha-lytic protease complexed with its pro region. Nat Struct Biol. 1998 Nov;5(11):945-50. PMID:9808037 doi:http://dx.doi.org/10.1038/2919

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