Crystallization, Crystal Structure Analysis and Atomic Model of the Complex Formed by a Human Fc Fragment and Fragment B of Protein A from<i>Staphylococcus aureus</i>

Deisenhofer, Johann; Jones, Thomas A.; Huber, Robert; Sjödahl, Jörgen; Sjöquist, John

doi:10.1515/bchm2.1978.359.2.975

Cited by 173 publications

(78 citation statements)

References 7 publications

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“…We prefer a model in which the C-terminal sections of the repeats form into helical bundles, the helices being interconnected by diverged loops. This hypothesis is consistent with the amphipathic property of the putative a-helical sections of the repeats and with the reported interdependence of the repeats for function and for folding [20,21]. As noted above, structure prediction suggests that the helical segment is interrupted at position 10 ( Fig.…”

Section: Discussionsupporting

confidence: 89%

The Drosophila ankyrin repeat protein cactus has a predominantly α‐helical secondary structure

Ntwasa

1993

FEBS Letters

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The cactus protein is the Drosophila homologue of the mammalian IKB family of cytoplasmic anchor proteins. We have expressed in E. cob and purified a cactus fusion protein, CACT-Bgl. CACT-Bgl protein contains the six ankyrin repeat sequences which are necessary for specific binding to the Drosophila rel family transcription factor dorsal. We show that the purified CACT-Bgl protein can bind specifically to dorsal and, using circular dichroism spectroscopy, that the protein adopts a largely a-helical secondary structure. A further analysis of the ankyrin repeat domains of cactus, using an improved secondary structure prediction program indicates that the N-terminal of the repeat will form into a loop structure and the C-terminal section into an interrupted, amphipathic a-helix. On the basis of these findings we propose that the ankyrin repeats of cactus fold together into helical bundles interconnected by diverged loops.

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Section: Discussionsupporting

confidence: 89%

The Drosophila ankyrin repeat protein cactus has a predominantly α‐helical secondary structure

Ntwasa

1993

FEBS Letters

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“…Usually the automated refinement reached a local minimum of crystallographic R value after about five cycles. In order to correct the model, Fourier maps mostly of the (2) F, I -IF, I) type, using calculated, combined [24] or Sim-weighted [25] phases were inspected in a Vector General graphics display system [26]. In the phase combination procedure, model phases calculated from the current models and multiple isomorphous replacement phases were given equal weights.…”

Section: X-ray Intensity Data Collection and Statisticsmentioning

confidence: 99%

The Refined Structure of the Selenoenzyme Glutathione Peroxidase at 0.2‐nm Resolution

Epp

Ladenstein

Wendel

1983

European Journal of Biochemistry

657

451

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The crystal structure of bovine erythrocyte glutathione peroxidase has been refined by a combined procedure of restrained crystallographic refinement and energy minimization at 0.20 nm resolution. The final R value at this resolution is 0.178. The r.m.s. deviation of main-chain atoms of the two independently refined monomers is 0.019 nm. The structure at 0.28 nm resolution, which has been determined by multiple isomorphous replacement, served as a starting model.The refined model allowed a detailed survey of the hydrogen-bonding pattern and of the subunit contact areas in the molecule. The model contains 165 solvent molecules per dimer, all taken as water molecules. The mobility of the structure was derived from the individual atomic temperature factors. The complete tetramer, including the active sites, seems to be rather rigid, except for narrow loops near to the N-terminal ends and some p turns exposed to solvent.The active centres of glutathione peroxidase are found in flat depressions on the molecular surface. The catalytically active selenocysteine residues could be located at the N-terminal ends of a helices forming /YG$ substructures together with two adjacent parallel p strands. In the vicinity of the reactive group some aromatic amino acid side-chains could be localized. Especially Trp-148, which could be hydrogen bonded to SeCys-35, may play a functional role during catalysis.The results ofsubstrate and inhibitor binding studies in solution and in the crystalline state could be interpreted by an apparent half-site reactivity of glutathione peroxidase. The enzyme seems to react in the sense of negative cooperativity with dimers being the functional units.Based on difference Fourier analyses of appropriate derivatives a reasonable model of glutathione binding is presented. Among the residues which could be of functional importance are Arg-40, Gln-130 and Arg-167, presumably forming salt bridges and a hydrogen bond to the glutathione molecule.In conclusion, a general picture of a minimal reaction mechanism, which is in good agreement with functional and structural data, is proposed. The main reaction of the catalytic cycle presumably shuttles between the selenolate and the selenenic acid state of SeCys-35.

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“…In this study we did not determine the subclass(es) of IgG that are present on human AM, and no data is available on the subclass specificities of the IgG receptor of AM (43)(44)(45). Interestingly, injury to human platelets by S. aureus has recently been shown also to involve interactions of cell wall protein A, IgG, and platelet Fc receptors (46).…”

Section: Discussionmentioning

confidence: 99%

Human alveolar macrophage cytophilic immunoglobulin G-mediated phagocytosis of protein A-positive staphylococci.

et al. 1982

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Crystallization, Crystal Structure Analysis and Atomic Model of the Complex Formed by a Human Fc Fragment and Fragment B of Protein A fromStaphylococcus aureus

Cited by 173 publications

References 7 publications

The Drosophila ankyrin repeat protein cactus has a predominantly α‐helical secondary structure

The Drosophila ankyrin repeat protein cactus has a predominantly α‐helical secondary structure

The Refined Structure of the Selenoenzyme Glutathione Peroxidase at 0.2‐nm Resolution

Human alveolar macrophage cytophilic immunoglobulin G-mediated phagocytosis of protein A-positive staphylococci.

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