1b65: Difference between revisions

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[[Image:1b65.gif|left|200px]]<br /><applet load="1b65" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1b65.gif|left|200px]]<br /><applet load="1b65" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1b65, resolution 1.82Å" />

'''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'''<br />

==Overview==

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.

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.

==About this Structure==

1B65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1B65 OCA].

1B65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B65 OCA].

==Reference==

Line 13:

[[Category: Ochrobactrum anthropi]]

[[Category: Single protein]]

[[Category: Beeumen, J.Van.]]

[[Category: Beeumen, J Van.]]

[[Category: Bompard-Gilles, C.]]

[[Category: Davies, G.J.]]

[[Category: Davies, G J.]]

[[Category: Fanuel, L.]]

[[Category: Frere, J.M.]]

[[Category: Frere, J M.]]

[[Category: Joris, B.]]

[[Category: Villeret, V.]]

Line 24:

[[Category: peptide degradation]]

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@@ Line 1: / Line 1: @@
-[[Image:1b65.gif|left|200px]]<br /><applet load="1b65" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1b65.gif|left|200px]]<br /><applet load="1b65" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1b65, resolution 1.82&Aring;" />
 '''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'''<br />
 ==Overview==
-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.
+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.
 ==About this Structure==
-B65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B65 OCA].
+B65 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ochrobactrum_anthropi Ochrobactrum anthropi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B65 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Ochrobactrum anthropi]]
 [[Category: Single protein]]
-[[Category: Beeumen, J.Van.]]
+[[Category: Beeumen, J Van.]]
 [[Category: Bompard-Gilles, C.]]
-[[Category: Davies, G.J.]]
+[[Category: Davies, G J.]]
 [[Category: Fanuel, L.]]
-[[Category: Frere, J.M.]]
+[[Category: Frere, J M.]]
 [[Category: Joris, B.]]
 [[Category: Villeret, V.]]
@@ Line 24: / Line 24: @@
 [[Category: peptide degradation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:46:47 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:51:53 2008''