1a16
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The structure of the proline-specific aminopeptidase (EC 3.4.11.9) from | + | The structure of the proline-specific aminopeptidase (EC 3.4.11.9) from Escherichia coli has been solved and refined for crystals of the native enzyme at a 2.0-A resolution, for a dipeptide-inhibited complex at 2.3-A resolution, and for a low-pH inactive form at 2.7-A resolution. The protein crystallizes as a tetramer, more correctly a dimer of dimers, at both high and low pH, consistent with observations from analytical ultracentrifuge studies that show that the protein is a tetramer under physiological conditions. The monomer folds into two domains. The active site, in the larger C-terminal domain, contains a dinuclear manganese center in which a bridging water molecule or hydroxide ion appears poised to act as the nucleophile in the attack on the scissile peptide bond of Xaa-Pro. The metal-binding residues are located in a single subunit, but the residues surrounding the active site are contributed by three subunits. The fold of the protein resembles that of creatine amidinohydrolase (creatinase, not a metalloenzyme). The C-terminal catalytic domain is also similar to the single-domain enzyme methionine aminopeptidase that has a dinuclear cobalt center. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xaa-Pro aminopeptidase]] | [[Category: Xaa-Pro aminopeptidase]] | ||
| - | [[Category: Bond, C | + | [[Category: Bond, C S.]] |
| - | [[Category: Dixon, N | + | [[Category: Dixon, N E.]] |
| - | [[Category: Freeman, H | + | [[Category: Freeman, H C.]] |
| - | [[Category: Guss, J | + | [[Category: Guss, J M.]] |
| - | [[Category: Lilley, P | + | [[Category: Lilley, P E.]] |
| - | [[Category: Wilce, M | + | [[Category: Wilce, M C.]] |
[[Category: MN]] | [[Category: MN]] | ||
[[Category: complex (proline peptidase/inhibitor)]] | [[Category: complex (proline peptidase/inhibitor)]] | ||
[[Category: proline peptidase]] | [[Category: proline peptidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:42 2008'' |
Revision as of 09:39, 21 February 2008
|
AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU
Overview
The structure of the proline-specific aminopeptidase (EC 3.4.11.9) from Escherichia coli has been solved and refined for crystals of the native enzyme at a 2.0-A resolution, for a dipeptide-inhibited complex at 2.3-A resolution, and for a low-pH inactive form at 2.7-A resolution. The protein crystallizes as a tetramer, more correctly a dimer of dimers, at both high and low pH, consistent with observations from analytical ultracentrifuge studies that show that the protein is a tetramer under physiological conditions. The monomer folds into two domains. The active site, in the larger C-terminal domain, contains a dinuclear manganese center in which a bridging water molecule or hydroxide ion appears poised to act as the nucleophile in the attack on the scissile peptide bond of Xaa-Pro. The metal-binding residues are located in a single subunit, but the residues surrounding the active site are contributed by three subunits. The fold of the protein resembles that of creatine amidinohydrolase (creatinase, not a metalloenzyme). The C-terminal catalytic domain is also similar to the single-domain enzyme methionine aminopeptidase that has a dinuclear cobalt center.
About this Structure
1A16 is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Xaa-Pro aminopeptidase, with EC number 3.4.11.9 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli., Wilce MC, Bond CS, Dixon NE, Freeman HC, Guss JM, Lilley PE, Wilce JA, Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3472-7. PMID:9520390
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