1tfu

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[[Image:1tfu.gif|left|200px]]
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{{STRUCTURE_1tfu| PDB=1tfu | SCENE= }}
{{STRUCTURE_1tfu| PDB=1tfu | SCENE= }}
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'''phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis'''
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===phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis===
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==Overview==
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Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in prokaryotic coenzyme A (CoA) biosynthesis, directing the transfer of an adenylyl group from ATP to 4'-phosphopantetheine (Ppant) to yield dephospho-CoA (dPCoA). The crystal structures of Escherichia coli PPAT bound to its substrates, product, and inhibitor revealed an allosteric hexameric enzyme with half-of-sites reactivity, and established an in-line displacement catalytic mechanism. To provide insight into the mechanism of ligand binding we solved the apoenzyme (Apo) crystal structure of PPAT from Mycobacterium tuberculosis. In its Apo form, PPAT is a symmetric hexamer with an open solvent channel. However, ligand binding provokes asymmetry and alters the structure of the solvent channel, so that ligand binding becomes restricted to one trimer.
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(as it appears on PubMed at http://www.pubmed.gov), where 15322293 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15322293}}
==About this Structure==
==About this Structure==
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[[Category: Tbsgc]]
[[Category: Tbsgc]]
[[Category: Transport protein]]
[[Category: Transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:54:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:14:49 2008''

Revision as of 09:14, 28 July 2008

Template:STRUCTURE 1tfu

phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis

Template:ABSTRACT PUBMED 15322293

About this Structure

1TFU is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Substrate-induced asymmetry and channel closure revealed by the apoenzyme structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase., Morris VK, Izard T, Protein Sci. 2004 Sep;13(9):2547-52. PMID:15322293

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