1war: Difference between revisions

Revision as of 19:52, 27 July 2008

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File:1war.png

Template:STRUCTURE 1war

RECOMBINANT HUMAN PURPLE ACID PHOSPHATASE EXPRESSED IN PICHIA PASTORISRECOMBINANT HUMAN PURPLE ACID PHOSPHATASE EXPRESSED IN PICHIA PASTORIS

Template:ABSTRACT PUBMED 15993892

About this StructureAbout this Structure

1WAR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''RECOMBINANT HUMAN PURPLE ACID PHOSPHATASE EXPRESSED IN PICHIA PASTORIS'''
+===RECOMBINANT HUMAN PURPLE ACID PHOSPHATASE EXPRESSED IN PICHIA PASTORIS===
-==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.
+The line below this paragraph, {{ABSTRACT_PUBMED_15993892}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15993892}}
 ==About this Structure==
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 [[Category: Tartrate resistant acid phosphatase]]
 [[Category: Uteroferrin]]
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