2bhb: Difference between revisions
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[[Category: proline-specific peptidase]] | [[Category: proline-specific peptidase]] | ||
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Revision as of 17:33, 30 October 2007
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ZN SUBSTITUTED E. COLI AMINOPEPTIDASE P
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
2BHB is a [Single protein] structure of sequence from [Escherichia coli] with ZN, FLC, MG and MRD 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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