1h3d

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{{STRUCTURE_1h3d| PDB=1h3d | SCENE= }}
{{STRUCTURE_1h3d| PDB=1h3d | SCENE= }}
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'''STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE'''
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===STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE===
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==Overview==
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ATP-phosphoribosyltransferase (ATP-PRT), the first enzyme of the histidine pathway, is a complex allosterically regulated enzyme, which controls the flow of intermediates through this biosynthetic pathway. The crystal structures of Escherichia coli ATP-PRT have been solved in complex with the inhibitor AMP at 2.7A and with product PR-ATP at 2.9A (the ribosyl-triphosphate could not be resolved). On the basis of binding of AMP and PR-ATP and comparison with type I PRTs, the PRPP and parts of the ATP-binding site are identified. These structures clearly identify the AMP as binding in the 5-phosphoribosyl-alpha-1-pyrophosphate (PRPP)-binding site, with the adenosine ring occupying the ATP-binding site. Comparison with the recently solved Mycobacterium tuberculosis ATP-PRT structures indicates that histidine is solely responsible for the large conformational changes observed between the hexameric forms of the enzyme. The role of oligomerisation in inhibition and the structural basis for the synergistic inhibition by histidine and AMP are discussed.
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(as it appears on PubMed at http://www.pubmed.gov), where 14741209 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14741209}}
==About this Structure==
==About this Structure==
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[[Category: Phosphoribosyltransferase]]
[[Category: Phosphoribosyltransferase]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:33:36 2008''

Revision as of 03:33, 1 July 2008

Template:STRUCTURE 1h3d

STRUCTURE OF THE E.COLI ATP-PHOSPHORIBOSYLTRANSFERASE

Template:ABSTRACT PUBMED 14741209

About this Structure

1H3D is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition., Lohkamp B, McDermott G, Campbell SA, Coggins JR, Lapthorn AJ, J Mol Biol. 2004 Feb 6;336(1):131-44. PMID:14741209

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