2bq8
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The crystal structure of human purple acid phosphatase recombinantly | + | The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution. In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III). The main difference between the two structures is the conformation of the enzyme "repression loop". Proteolytic cleavage of this loop in vivo or in vitro results in significant activation of the mammalian PAPs. In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex. The carboxylate side-chain of Asp145 and the neighboring Phe146 side-chain thus block the active site, thereby inactivating the enzyme. In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures. The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop. |
==About this Structure== | ==About this Structure== | ||
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[[Category: trap]] | [[Category: trap]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:30 2008'' |
Revision as of 14:40, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN PURPLE ACID PHOSPHATASE WITH AN INHIBITORY CONFORMATION OF THE REPRESSION LOOP
Overview
The crystal structure of human purple acid phosphatase recombinantly expressed in Escherichia coli (rHPAP(Ec)) and Pichia pastoris (rHPAP(Pp)) has been determined in two different crystal forms, both at 2.2A resolution. In both cases, the enzyme crystallized in its oxidized (inactive) state, in which both Fe atoms in the dinuclear active site are Fe(III). The main difference between the two structures is the conformation of the enzyme "repression loop". Proteolytic cleavage of this loop in vivo or in vitro results in significant activation of the mammalian PAPs. In the crystals obtained from rHPAP(Ec), the carboxylate side-chain of Asp145 of this loop acts as a bidentate ligand that bridges the two metal atoms, in a manner analogous to a possible binding mode for a phosphate ester substrate in the enzyme-substrate complex. The carboxylate side-chain of Asp145 and the neighboring Phe146 side-chain thus block the active site, thereby inactivating the enzyme. In the crystal structure of rHPAP(Pp), the enzyme "repression loop" has an open conformation similar to that observed in other mammalian PAP structures. The present structures demonstrate that the repression loop exhibits significant conformational flexibility, and the observed alternate binding mode suggests a possible inhibitory role for this loop.
About this Structure
2BQ8 is a Single protein structure of sequence from Homo sapiens with , and as ligands. Active as Acid phosphatase, with EC number 3.1.3.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop., Strater N, Jasper B, Scholte M, Krebs B, Duff AP, Langley DB, Han R, Averill BA, Freeman HC, Guss JM, J Mol Biol. 2005 Aug 5;351(1):233-46. Epub 2005 Apr 26. PMID:15993892
Page seeded by OCA on Thu Feb 21 16:40:30 2008
Categories: Acid phosphatase | Homo sapiens | Single protein | Jasper, B. | Krebs, B. | Straeter, N. | FE2 | SO4 | ZN | Dinuclear metal site | Hydrolase | Metallophosphatase | Trap
