Alpha-lytic protease: Difference between revisions

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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>
'''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>
*<scene name='55/551214/Cv/2'>ALP protease domain and pro domain complex with benzenesulfonyl fluoride</scene>.
*<scene name='55/551214/Cv/4'>ALP protease domain and pro domain complex with benzenesulfonyl fluoride</scene>. Water molecules are shown as red spheres.
<scene name='55/551214/Cv/3'>Benzenesulfonyl fluoride binding site</scene> (PDB entry [[3pro]]).
*<scene name='55/551214/Cv/5'>Benzenesulfonyl fluoride binding site</scene> (PDB entry [[3pro]]).<ref>PMID:9808037</ref>  
</StructureSection>


== 3D Structures of alpha-lytic protease ==
== 3D Structures of alpha-lytic protease ==
[[Alpha-lytic protease 3D structures]]


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
</StructureSection>
{{#tree:id=OrganizedByTopic|openlevels=0|
 
*ALP protease domain
 
**[[2alp]], [[1p09]], [[1tal]], [[2ull]], [[1boq]], [[1ssz]], [[2h5c]], [[1ssx]] – LeALP – ''Lysobacter enzymogenes''  <BR />
**[[1gba]], [[1gbe]], [[1gbj]], [[3urc]], [[3urd]], [[3ure]], [[1qq4]] – LeALP (mutant)  <BR />
**[[1p01]], [[1p02]], [[1p03]], [[1p04]], [[1p05]], [[1p06]], [[1p10]], [[2lpr]], [[3lpr]], [[5lpr]], [[6lpr]], [[7lpr]], [[8lpr]], [[9lpr]], [[2h5d]] – LeALP + boronic acid inhibitor  <BR />
**[[1gbb]], [[1gbc]], [[1gbd]], [[1gbf]], [[1gbh]], [[1gbi]], [[1gbk]], [[1gbl]], [[1gbm]] – LeALP (mutant) + boronic acid inhibitor  <BR />
**[[1p11]], [[1p12]] – LeALP + phosphonate esther inhibitor  <BR />
**[[3qgj]] – LeALP + peptide  <BR />
 
*ALP pro region
 
**[[2pro]], [[1qrx]] – LeALP pro region  <BR />
**[[1qrw]], [[3m7t]], [[3m7u]] – LeALP pro region (mutant) <BR />
 
*ALP pro+protease domains
 
**[[3pro]], [[4pro]] – LeALP (mutant)  <BR />


}}
== References ==
== References ==
<references/>
<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

Latest revision as of 11:31, 6 March 2019


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)

Drag the structure with the mouse to rotate

ReferencesReferences

  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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Michal Harel, Alexander Berchansky
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