1tfu
From Proteopedia
(New page: 200px<br /><applet load="1tfu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tfu, resolution 1.99Å" /> '''phosphopantetheine a...) |
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| - | [[Image:1tfu.gif|left|200px]]<br /><applet load="1tfu" size=" | + | [[Image:1tfu.gif|left|200px]]<br /><applet load="1tfu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tfu, resolution 1.99Å" /> | caption="1tfu, resolution 1.99Å" /> | ||
'''phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis'''<br /> | '''phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1TFU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase Pantetheine-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3] Full crystallographic information is available from [http:// | + | 1TFU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Active as [http://en.wikipedia.org/wiki/Pantetheine-phosphate_adenylyltransferase Pantetheine-phosphate adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.3 2.7.7.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Izard, T.]] | [[Category: Izard, T.]] | ||
| - | [[Category: Morris, V | + | [[Category: Morris, V K.]] |
| - | [[Category: TBSGC, TB | + | [[Category: TBSGC, TB Structural Genomics Consortium.]] |
[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
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[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:05 2008'' |
Revision as of 13:13, 21 February 2008
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phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis
Overview
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.
About this Structure
1TFU is a Single protein structure of sequence from Mycobacterium tuberculosis. Active as Pantetheine-phosphate adenylyltransferase, with EC number 2.7.7.3 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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