2bha: Difference between revisions
New page: left|200px<br /> <applet load="2bha" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bha, resolution 2.40Å" /> '''E. COLI AMINOPEPTID... |
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==About this Structure== | ==About this Structure== | ||
2BHA is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with FLC and MG as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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=2BHA OCA]]. | 2BHA is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with FLC and MG as [[http://en.wikipedia.org/wiki/ligands ligands]]. 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: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BHA OCA]]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Xaa-Pro aminopeptidase]] | |||
[[Category: Bond, C.S.]] | [[Category: Bond, C.S.]] | ||
[[Category: Freeman, H.C.]] | [[Category: Freeman, H.C.]] | ||
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[[Category: substrate complex]] | [[Category: substrate complex]] | ||
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Revision as of 13:17, 30 October 2007
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E. COLI AMINOPEPTIDASE P IN COMPLEX WITH SUBSTRATE
OverviewOverview
The effect of metal substitution on the activity and structure of the, aminopeptidase P (APPro) from Escherichia coli has been investigated., Measurements of activity in the presence of Mn2+, Mg2+, Zn2+, Na+, and, Ca2+ show that significant activity is seen only in the Mn-bound form of, the enzyme. The addition of Zn2+ to [MnMn(APPro)] is strongly inhibitory., Crystal structures of [MnMn(APPro)], [MgMg(APPro)], [ZnZn(APPro)], [ZnMg(APPro)], [Ca_(APPro)], [Na_(APPro)], and [apo(APPro)] were, determined. The structures of [Ca_(APPro)] and [Na_(APPro)] have a single, metal atom at their active site. Surprisingly, when a tripeptide substrate, (ValProLeu) was soaked into [Na_(APPro)] crystals in the presence of 200, mM Mg2+, the structure had substrate, but no metal, bound at the active, site. ... [(full description)]
About this StructureAbout this Structure
2BHA is a [Protein complex] structure of sequences from [Escherichia coli] with FLC and MG as [ligands]. Active as [Xaa-Pro aminopeptidase], with EC number [3.4.11.9]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center., Graham SC, Bond CS, Freeman HC, Guss JM, Biochemistry. 2005 Oct 25;44(42):13820-36. PMID:16229471
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