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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 10
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pubmed:dateCreated |
2004-9-24
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pubmed:abstractText |
Aminopeptidase P (APPro) is a metalloprotease whose active site includes a dinuclear manganese(II) cluster. The enzyme cleaves the N-terminal residue from a polypeptide when the second residue is proline. A complex of Escherichia coli APPro (EcAPPro) with an inhibitor, apstatin [N-(2S,3R)-3-amino-2-hydroxy-4-phenyl-butanoyl-L-prolyl-L-prolyl-L-alaninamide], has been crystallized. Apstatin binds to the active site of EcAPPro with its N-terminal amino group coordinated to one of the two Mn(II) atoms at the metal centre. The apstatin hydroxyl group replaces a hydroxide ion which bridges the two metal atoms in the native enzyme. The first proline residue of apstatin lies in a small hydrophobic cleft. The structure of the apstatin-EcAPPro complex has been refined at 2.3 A resolution with residuals R = 0.179 and R(free) = 0.204. The structure of the complex illustrates how apstatin inhibits APPro and suggests how substrates may bind to the enzyme, but the basis of the proline-specificity remains elusive.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0907-4449
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1770-9
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pubmed:dateRevised |
2007-7-24
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pubmed:meshHeading |
pubmed-meshheading:15388923-Amino Acid Sequence,
pubmed-meshheading:15388923-Aminopeptidases,
pubmed-meshheading:15388923-Binding Sites,
pubmed-meshheading:15388923-Catalysis,
pubmed-meshheading:15388923-Crystallography, X-Ray,
pubmed-meshheading:15388923-Escherichia coli,
pubmed-meshheading:15388923-Hydroxides,
pubmed-meshheading:15388923-Ions,
pubmed-meshheading:15388923-Manganese,
pubmed-meshheading:15388923-Models, Chemical,
pubmed-meshheading:15388923-Models, Molecular,
pubmed-meshheading:15388923-Molecular Sequence Data,
pubmed-meshheading:15388923-Peptides,
pubmed-meshheading:15388923-Proline,
pubmed-meshheading:15388923-Protein Binding,
pubmed-meshheading:15388923-Protein Conformation,
pubmed-meshheading:15388923-Protein Structure, Secondary,
pubmed-meshheading:15388923-Protein Structure, Tertiary,
pubmed-meshheading:15388923-Sequence Homology, Amino Acid,
pubmed-meshheading:15388923-Software
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pubmed:year |
2004
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pubmed:articleTitle |
Structure of Escherichia coli aminopeptidase P in complex with the inhibitor apstatin.
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pubmed:affiliation |
School of Molecular and Microbial Biosciences, University of Sydney, NSW 2006, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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