1tfu
From Proteopedia
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| - | [[Image:1tfu.gif|left|200px]] | + | [[Image:1tfu.gif|left|200px]] |
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| - | '''phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis''' | + | {{Structure |
| + | |PDB= 1tfu |SIZE=350|CAPTION= <scene name='initialview01'>1tfu</scene>, resolution 1.99Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= COAD, KDTB, RV2965C, MT3043, MTCY349.22, U0002E, MB2989C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
| + | }} | ||
| + | |||
| + | '''phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TFU is a [ | + | 1TFU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFU OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15322293 15322293] |
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Pantetheine-phosphate adenylyltransferase]] | [[Category: Pantetheine-phosphate adenylyltransferase]] | ||
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[[Category: protein structure initiative]] | [[Category: protein structure initiative]] | ||
[[Category: psi]] | [[Category: psi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: tb structural genomics consortium]] | [[Category: tb structural genomics consortium]] | ||
[[Category: tbsgc]] | [[Category: tbsgc]] | ||
[[Category: transport protein]] | [[Category: transport protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:17:50 2008'' |
Revision as of 12:17, 20 March 2008
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| , resolution 1.99Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | COAD, KDTB, RV2965C, MT3043, MTCY349.22, U0002E, MB2989C (Mycobacterium tuberculosis) | ||||||
| Activity: | Pantetheine-phosphate adenylyltransferase, with EC number 2.7.7.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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