1o78 | pdb_00001o78

BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (1.3S) [10-48] DELETION MUTANT

spinqualitylabelsall models 1o78, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1o78 is a 1 chain structure with sequence from "propionibacterium_shermanii"_van_niel_1928 "propionibacterium shermanii" van niel 1928. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1dcz, 1dd2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [BCCP_PROFR] The biotinyl 1.3S subunit serves as a carboxyl carrier between the substrate-binding sites on the 12S and 5S subunits. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed A deletion mutant of the transcarboxylase biotin carrier protein was completely labeled with 13C and 15N. A multitude of 2D and 3D NMR spectra were recorded and assigned. An NMR solution structure was derived from the data and compared in detail with the recently published structure of the wild-type. It is shown that deletion of 30% of the amino acids does not alter the structure of the rigid protein core. NMR studies on the solution structure of a deletion mutant of the transcarboxylase biotin carrier subunit.,Jank MM, Sadowsky JD, Peikert C, Berger S Int J Biol Macromol. 2002 Oct 1;30(5):233-42. PMID:12297230 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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