Source:http://linkedlifedata.com/resource/pubmed/id/16885166
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
44
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| pubmed:dateCreated |
2006-10-30
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| pubmed:databankReference | |
| pubmed:abstractText |
Aminopeptidase N from Escherichia coli is a broad specificity zinc exopeptidase belonging to aminopeptidase clan MA, family M1. The structures of the ligand-free form and the enzyme-bestatin complex were determined at 1.5- and 1.6-A resolution, respectively. The enzyme is composed of four domains: an N-terminal beta-domain (Met(1)-Asp(193)), a catalytic domain (Phe(194)-Gly(444)), a middle beta-domain (Thr(445)-Trp(546)), and a C-terminal alpha-domain (Ser(547)-Ala(870)). The structure of the catalytic domain exhibits similarity to thermolysin, and a metal-binding motif (HEXXHX(18)E) is found in the domain. The zinc ion is coordinated by His(297), His(301), Glu(320), and a water molecule. The groove on the catalytic domain that contains the active site is covered by the C-terminal alpha-domain, and a large cavity is formed inside the protein. However, there exists a small hole at the center of the C-terminal alpha-domain. The N terminus of bestatin is recognized by Glu(121) and Glu(264), which are located in the N-terminal and catalytic domains, respectively. Glu(298) and Tyr(381), located near the zinc ion, are considered to be involved in peptide cleavage. A difference revealed between the ligand-free form and the enzyme-bestatin complex indicated that Met(260) functions as a cushion to accept substrates with different N-terminal residue sizes, resulting in the broad substrate specificity of this enzyme.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD13,
http://linkedlifedata.com/resource/pubmed/chemical/Leucine,
http://linkedlifedata.com/resource/pubmed/chemical/Methionine,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/bestatin
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| pubmed:status |
MEDLINE
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| pubmed:month |
Nov
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
3
|
| pubmed:volume |
281
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
33664-76
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| pubmed:meshHeading |
pubmed-meshheading:16885166-Amino Acid Sequence,
pubmed-meshheading:16885166-Antigens, CD13,
pubmed-meshheading:16885166-Binding Sites,
pubmed-meshheading:16885166-Catalysis,
pubmed-meshheading:16885166-Crystallography, X-Ray,
pubmed-meshheading:16885166-Escherichia coli,
pubmed-meshheading:16885166-Gene Expression,
pubmed-meshheading:16885166-Humans,
pubmed-meshheading:16885166-Leucine,
pubmed-meshheading:16885166-Methionine,
pubmed-meshheading:16885166-Models, Molecular,
pubmed-meshheading:16885166-Molecular Sequence Data,
pubmed-meshheading:16885166-Plasmids,
pubmed-meshheading:16885166-Protein Structure, Quaternary,
pubmed-meshheading:16885166-Protein Structure, Tertiary,
pubmed-meshheading:16885166-Protein Subunits,
pubmed-meshheading:16885166-Sequence Alignment,
pubmed-meshheading:16885166-Structural Homology, Protein,
pubmed-meshheading:16885166-Substrate Specificity
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| pubmed:year |
2006
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| pubmed:articleTitle |
Crystal structure of aminopeptidase N (proteobacteria alanyl aminopeptidase) from Escherichia coli and conformational change of methionine 260 involved in substrate recognition.
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| pubmed:affiliation |
Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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