1a16
From Proteopedia
(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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==About this Structure== | ==About this Structure== | ||
| - | 1A16 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with MN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A16 OCA]]. | + | 1A16 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with MN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9]]. Structure known Active Site: NUL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A16 OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Xaa-Pro aminopeptidase]] | ||
[[Category: Bond, C.S.]] | [[Category: Bond, C.S.]] | ||
[[Category: Dixon, N.E.]] | [[Category: Dixon, N.E.]] | ||
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[[Category: proline peptidase]] | [[Category: proline peptidase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:33:50 2007'' |
Revision as of 10:29, 30 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 [Xaa-Pro aminopeptidase], with EC number [3.4.11.9]. Structure known Active Site: NUL. 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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