1a16

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{{STRUCTURE_1a16| PDB=1a16 | SCENE= }}
{{STRUCTURE_1a16| PDB=1a16 | SCENE= }}
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'''AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU'''
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===AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9520390 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9520390}}
==About this Structure==
==About this Structure==
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[[Category: Wilce, M C.]]
[[Category: Wilce, M C.]]
[[Category: Proline peptidase]]
[[Category: Proline peptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:46:01 2008''

Revision as of 12:46, 30 June 2008

Image:1a16.png

Template:STRUCTURE 1a16

AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU

Template:ABSTRACT PUBMED 9520390

About this Structure

1A16 is a Single protein structure of sequence from Escherichia coli. 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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