Alpha-lytic protease

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<StructureSection load='3pro' size='350' side='right' caption='Structure of alpha-lytic protease protease domain (grey, green) and pro domain (yellow, pink) complex with benzenesulfonyl fluoride (PDB entry [[3pro]])' scene=''>
<StructureSection load='3pro' size='350' side='right' caption='Structure of alpha-lytic protease protease domain (grey, green) and pro domain (yellow, pink) complex with benzenesulfonyl fluoride (PDB entry [[3pro]])' scene=''>
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'''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).
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'''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).<ref>PMID:2611204</ref>
</StructureSection>
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== References ==
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<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

Revision as of 11:28, 3 December 2015

Structure of alpha-lytic protease protease domain (grey, green) and pro domain (yellow, pink) complex with benzenesulfonyl fluoride (PDB entry 3pro)

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3D Structures of alpha-lytic protease

Updated on 03-December-2015

References

  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

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Michal Harel, Alexander Berchansky

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