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Journal Issue - Volume 5 Issue 11 (November 1996)

Abstract UDP‐galactose 4‐epimerase from Escherichia coli catalyzes the interconversion of UDP‐glucose and UDP‐galactose. In recent years, the enzyme has been the subject of intensive investigation due in part to its ability to facilitate nonstereospecific hydride transfer between β‐NADH and a 4‐keto hexopyranose intermediate. The first molecular model of the epimerase from E. coli was solved to 2.5 Å resolution with crystals grown in the...

  • 9k and S100β

  • Barbara C.M. Potts, Göran Carlström, Katsuo Okazaki, Hiroyoshi Hidaka, Walter J. Chazin
  • Published in Wiley Interscience on Dec 31, 2008
  • DOI: 10.1002/pro.5560051103 (p 2162-2174)

Abstract The homodimeric S100 protein calcyclin has been studied in the apo state by two‐dimensional 1H NMR spectroscopy. Using a combination of scalar correlation and NOE experiments, sequence‐specific 1H NMR assignments were obtained for all but one backbone and >90% of the side‐chain resonances. To our knowledge, the 2 × 90 residue (20 kDa) calcyclin dimer is the largest protein system for which such complete assignments have been made by purely ...

Abstract Stellacyanins are blue (type I) copper glycoproteins that differ from other members of the cupredoxin family in their spectroscopic and electron transfer properties. Until now, stellacyanins have eluded structure determination. Here we report the three‐dimensional crystal structure of the 109 amino acid, non‐glycosylated copper binding domain of recombinant cucumber stellacyanin refined to 1.6 Å resolution. The...

Abstract The cDNA encoding the 182 amino acid long precursor stellacyanin from Cucumis sativus was isolated and characterized. The protein precursor consists of four sequence domains: I, a 23 amino acid hydrophobic N‐terminal signal peptide with features characteristic of secretory proteins; II, a 109 amino acid copper‐binding domain; III, a 26 amino acid hydroxyproline‐ and serine‐rich peptide characteristic of motifs found in the extensin...

  • Solution structure of a mini IGF‐1

  • Elke De Wolf, Raj Gill, Stella Geddes, Jim Pitts, Axel Wollmer, Joachim Grötzinger
  • Published in Wiley Interscience on Dec 31, 2008
  • DOI: 10.1002/pro.5560051106 (p 2193-2202)

Abstract Mini insulin‐like growth factor 1, an inactive insulin‐like growth factor 1 mutant lacking the C region, was studied by 2D NMR spectroscopy. Resonances were assigned for almost all protons of the 57 amino acid residues. The 3D structure of the protein was determined by distance geometry methods. Three helical segments; Ala 8‐Cys 18, Gly 42‐Phe 49, and Leu 54‐Cys 61, were identified, corresponding to those present in...

Abstract Picornaviral proteinases are responsible for maturation cleavages of the viral polyprotein, but also catalyze the degradation of cellular targets. Using graphical visualization techniques and neural network algorithms, we have investigated the sequence specificity of the two proteinases 2Apro and 3Cpro. The cleavage of VP0 (giving rise to VP2 and VP4), which is carried out by a so‐far unknown proteinase, was also examined. ...

Abstract We evaluate to what extent the structure of proteins can be deduced from incomplete knowledge of disulfide bridges, surface assignments, secondary structure assignments, and additional distance constraints. A cost function taking such constraints into account was used to obtain protein structures using a simple minimization algorithm. For small proteins, the approximate structure could be obtained using one additional...

Abstract Various conformational forms of the archetypal serpin human α1proteinase inhibitor (α1PI), including ordered polymers, active and inactive monomers, and heterogeneous aggregates, have been produced by refolding from mild denaturing conditions. These forms presumably originate by different folding pathways during renaturation, under the influence of the A and C sheets of the molecule. Because α1PI contains only two Trp residues, at...

Abstract Ecotin, a homodimeric protein composed of 142 residue subunits, is a novel serine protease inhibitor present in Escherichia coli. Its thermostability and acid stability, as well as broad specificity toward proteases, make it an interesting protein for structural characterization. Its structure in the uncomplexed state, determined for two different crystalline environments, allows a structural comparison of the free inhibitor with that...

Abstract The UV dynamic fluorescence and CD of several Pseudomonas aeruginosa azurins bearing single amino acid mutation have been studied. Two classes of mutants were examined. In the first class, two hydrophobic residues in the core of the protein, Ile 7 and Phe 110, nearest to the azurin single tryptophan Trp 48, were substituted by a serine (mutants I7S and F110S). In the second class, two residues in the outer sphere of the copper ligand...

Abstract Thermostability and unfolding behavior of the wild‐type (1,3–1,4)‐β‐glucanases from Bacillus macerans (MAC) and Bacillus amyloliquefaciens (AMY) and of two hybrid enzymes H(A12‐M)ΔF14 and H(A12‐M)ΔY13F14A were studied by spectroscopic and microcalorimetric measurements. H(A12‐M)ΔF14 is constructed by the fusion of 12 N‐terminal amino acids of AMY with amino acids 13–214 of MAC, and by deletion of F14. In H(A12‐M)ΔY13F14A, the...

Abstract The glutamic acid‐specific protease from Streptomyces griseus (SGPE) is an 18.4‐kDa serine protease with a distinct preference for Glu in the P1 position. Other enzymes characterized by a strong preference for negatively charged residues in the P1 position, e.g., interleukin‐1β converting enzyme (ICE), use Arg or Lys residues as counterions within the S1 binding site. However, in SGPE, this function is contributed by a His residue (His 213) and two Ser...

Abstract Aspartate transcarbamoylase from Escherichia coli shows homotropic cooperativity for aspartate as well as hetero‐tropic regulation by nucleotides. Structurally, it consists of two trimeric catalytic subunits and three dimeric regulatory subunits, each chain being comprised of two domains. Glu‐50 and Ser‐171 are involved in stabilizing the closed conformation of the catalytic chain. Replacement of Glu‐50 or Ser‐171 by Ala in...

Abstract The hydropathy plot of the inwardly rectifying ROMK1 K+ channel, which reveals two transmembrane and a pore region domains, also reveals areas of intermediate hydrophobicity in the N terminus (M0) and in the C terminus (post‐M2). Peptides that correspond to M0, post‐M2, and a control peptide, pre‐M0, were synthesized and characterized for their structure, affinity to phospholipid membranes, organizational state in membranes, ...

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