3pnb | pdb_00003pnb

Phosphopantetheine Adenylyltransferase from Mycobacterium tuberculosis in complex with coenzyme A

spinqualitylabelsall models 3pnb, resolution 2.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. Ligands: COA 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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