1gyt

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(New page: 200px<br /> <applet load="1gyt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gyt, resolution 2.5&Aring;" /> '''E. COLI AMINOPEPTIDA...)
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Revision as of 16:35, 29 October 2007

Image:1gyt.gif

1gyt, resolution 2.5Å

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E. COLI AMINOPEPTIDASE A (PEPA)

Overview

The structure of aminopeptidase A (PepA), which functions as a DNA-binding, protein in Xer site-specific recombination and in transcriptional control, of the carAB operon in Escherichia coli, has been determined at 2.5 A, resolution. In Xer recombination at cer, PepA and the arginine repressor, (ArgR) serve as accessory proteins, ensuring that recombination is, exclusively intramolecular. In contrast, PepA homologues from other, species have no known DNA-binding activity and are not implicated in, transcriptional regulation or control of site-specific recombination. PepA, comprises two domains, which have similar folds to the two domains of, bovine lens leucine aminopeptidase (LAP). However, the N-terminal domain, of PepA, which probably plays a significant role in DNA binding, is, ... [(full description)]

About this Structure

1GYT is a [Single protein] structure of sequence from [Escherichia coli] with ZN, CO3 and CL as [ligands]. Active as [[1]], with EC number [3.4.11.1]. Full crystallographic information is available from [OCA].

Reference

X-ray structure of aminopeptidase A from Escherichia coli and a model for the nucleoprotein complex in Xer site-specific recombination., Strater N, Sherratt DJ, Colloms SD, EMBO J. 1999 Aug 16;18(16):4513-22. PMID:10449417

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