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1b65

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{{STRUCTURE_1b65| PDB=1b65 | SCENE= }}
{{STRUCTURE_1b65| PDB=1b65 | SCENE= }}
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'''Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold'''
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===Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold===
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==Overview==
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Background: The L-aminopeptidase D-Ala-esterase/amidase from Ochrobactrum anthropi (DmpA) releases the N-terminal L and/or D-Ala residues from peptide substrates. This is the only known enzyme to liberate N-terminal amino acids with both D and L stereospecificity. The DmpA active form is an alphabeta heterodimer, which results from a putative autocatalytic cleavage of an inactive precursor polypeptide. Results: The crystal structure of the enzyme has been determined to 1.82 A resolution using the multiple isomorphous replacement method. The heterodimer folds into a single domain organised as an alphabetabetaalpha sandwich in which two mixed beta sheets are flanked on both sides by two alpha helices. Conclusions: DmpA shows no similarity to other known aminopeptidases in either fold or catalytic mechanism, and thus represents the first example of a novel family of aminopeptidases. The protein fold of DmpA does, however, show structural homology to members of the N-terminal nucleophile (Ntn) hydrolase superfamily. DmpA presents functionally equivalent residues in the catalytic centre when compared with other Ntn hydrolases, and is therefore likely to use the same catalytic mechanism. In spite of this homology, the direction and connectivity of the secondary structure elements differ significantly from the consensus Ntn hydrolase topology. The DmpA structure thus characterises a new subfamily, but supports the common catalytic mechanism for these enzymes suggesting an evolutionary relationship.
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(as it appears on PubMed at http://www.pubmed.gov), where 10673442 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10673442}}
==About this Structure==
==About this Structure==
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[[Category: Ntn hydrolase]]
[[Category: Ntn hydrolase]]
[[Category: Peptide degradation]]
[[Category: Peptide degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:07:08 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:21:20 2008''

Revision as of 15:21, 30 June 2008

Image:1b65.png

Template:STRUCTURE 1b65

Structure of l-aminopeptidase d-ala-esterase/amidase from ochrobactrum anthropi, a prototype for the serine aminopeptidases, reveals a new variant among the ntn hydrolase fold

Template:ABSTRACT PUBMED 10673442

About this Structure

1B65 is a Single protein structure of sequence from Ochrobactrum anthropi. Full crystallographic information is available from OCA.

Reference

A new variant of the Ntn hydrolase fold revealed by the crystal structure of L-aminopeptidase D-ala-esterase/amidase from Ochrobactrum anthropi., Bompard-Gilles C, Villeret V, Davies GJ, Fanuel L, Joris B, Frere JM, Van Beeumen J, Structure. 2000 Feb 15;8(2):153-62. PMID:10673442

Page seeded by OCA on Mon Jun 30 18:21:20 2008

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