6dnu

Crystal Structure of Neisseria meningitidis DsbD c-terminal domain in the oxidised formCrystal Structure of Neisseria meningitidis DsbD c-terminal domain in the oxidised form

Structural highlights 6dnu is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Activity: Protein-disulfide reductase, with EC number 1.8.1.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [C6S7X6_NEIML] Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps.[HAMAP-Rule:MF_00399] Publication Abstract from PubMed The membrane protein DsbD is a reductase that acts as an electron hub, translocating reducing equivalents from cytoplasmic thioredoxin to a number of periplasmic substrates involved in oxidative protein folding, cytochrome c maturation and oxidative stress defence. DsbD is a multi-domain protein consisting of a transmembrane domain (t-DsbD) flanked by two periplasmic domains (n-DsbD and c-DsbD). Previous studies have shown that DsbD is required for the survival of the obligate human pathogen Neisseria meningitidis. To help understand the structural and functional aspects of N. meningitidis DsbD, the two periplasmic domains which are required for electron transfer are being studied. Here, the expression, purification and biophysical properties of n-NmDsbD and c-NmDsbD are described. The crystallization and crystallographic analysis of n-NmDsbD and c-NmDsbD are also described in both redox states, which differ only in the presence or absence of a disulfide bond but which crystallized in completely different conditions. Crystals of n-NmDsbDOx, n-NmDsbDRed, c-NmDsbDOx and c-NmDsbDRed diffracted to 2.3, 1.6, 2.3 and 1.7 A resolution and belonged to space groups P213, P321, P41 and P1211, respectively. Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.,Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B Acta Crystallogr F Struct Biol Commun. 2018 Jan 1;74(Pt 1):31-38. doi:, 10.1107/S2053230X17017800. Epub 2018 Jan 1. PMID:29372905 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6dnu, resolution 2.28Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image