2laf

NMR solution structure of the N-terminal domain of the E. coli lipoprotein BamCNMR solution structure of the N-terminal domain of the E. coli lipoprotein BamC

Structural highlights 2laf is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. Related: 2lae Activity: Glucokinase, with EC number 2.7.1.2 Publication Abstract from PubMed The CS-RDC-NOE Rosetta program was used to generate the solution structure of a 27-kDa fragment of the Escherichia coli BamC protein from a limited set of NMR data. The BamC protein is a component of the essential five-protein beta-barrel assembly machine in E. coli. The first 100 residues in BamC were disordered in solution. The Rosetta calculations showed that BamC(101-344) forms two well-defined domains connected by an approximately 18-residue linker, where the relative orientation of the domains was not defined. Both domains adopt a helix-grip fold previously observed in the Bet v 1 superfamily. (15)N relaxation data indicated a high degree of conformational flexibility for the linker connecting the N-terminal domain and the C-terminal domain in BamC. The results here show that CS-RDC-NOE Rosetta is robust and has a high tolerance for misassigned nuclear Overhauser effect restraints, greatly simplifying NMR structure determinations. Structure of the BamC Two-Domain Protein Obtained by Rosetta with a Limited NMR Data Set.,Warner LR, Varga K, Lange OF, Baker SL, Baker D, Sousa MC, Pardi A J Mol Biol. 2011 Aug 5;411(1):83-95. Epub 2011 May 23. PMID:21624375 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2laf, 9 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image