Structural highlights
3pnb is a 4 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Related: | 3nba, 3nbk |
| Gene: | coaD, kdtB, Rv2965c, MT3043, MTCY349.22, u0002e ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) |
| Activity: | Pantetheine-phosphate adenylyltransferase, with EC number 2.7.7.3 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[COAD_MYCTU] Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (By similarity).
Publication Abstract from PubMed
Phosphopantetheine adenylyltransferase (PPAT) catalyzes the penultimate step in the coenzyme A (CoA) biosynthetic pathway, reversibly transferring an adenylyl group from ATP to 4'-phosphopantetheine to form dephosphocoenzyme A (dPCoA). To complement recent biochemical and structural studies on Mycobacterium tuberculosis PPAT (MtPPAT) and to provide further insight into the feedback regulation of MtPPAT by CoA, the X-ray crystal structure of the MtPPAT enzyme in complex with CoA was determined to 2.11 A resolution. Unlike previous X-ray crystal structures of PPAT-CoA complexes from other bacteria, which showed two distinct CoA conformations bound to the active site, only one conformation of CoA is observed in the MtPPAT-CoA complex.
Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation.,Wubben T, Mesecar AD Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):541-5. Epub 2011 Apr 20. PMID:21543857[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wubben T, Mesecar AD. Structure of Mycobacterium tuberculosis phosphopantetheine adenylyltransferase in complex with the feedback inhibitor CoA reveals only one active-site conformation. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt, 5):541-5. Epub 2011 Apr 20. PMID:21543857 doi:10.1107/S1744309111010761
