1a16: Difference between revisions

Revision as of 15:46, 30 June 2008

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File:1a16.png

Template:STRUCTURE 1a16

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

Template:ABSTRACT PUBMED 9520390

About this StructureAbout this Structure

1A16 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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-'''AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9520390}}, adds the Publication Abstract to the page
+(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==
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 [[Category: Wilce, M C.]]
 [[Category: Proline peptidase]]
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