1tfu
From Proteopedia
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| , resolution 1.99Å | |||||||
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| Gene: | COAD, KDTB, RV2965C, MT3043, MTCY349.22, U0002E, MB2989C (Mycobacterium tuberculosis) | ||||||
| Activity: | Pantetheine-phosphate adenylyltransferase, with EC number 2.7.7.3 | ||||||
| Domains: | PPAT_a | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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