1a16
From Proteopedia
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(New page: 200px<br /> <applet load="1a16" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a16, resolution 2.3Å" /> '''AMINOPEPTIDASE P FRO...)
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Revision as of 17:21, 29 October 2007
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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, ... [(full description)]
About this Structure
1A16 is a [Single protein] structure of sequence from [Escherichia coli] with MN as [ligand]. Active as [[1]], with EC number [3.4.11.9]. 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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