issue contents

Journal logoBIOLOGICAL
ISSN: 1399-0047

March 2009 issue

Highlighted illustration

Cover illustration: GlmU is the bifunctional acetyltransferase/uridyltransferase that catalyses the conversion of GlcN-1-P to UDP-GlcNAc, a key substrate in lipopolysaccharide and peptidoglycan synthesis. The cover figure shows the bio­logical trimer of the M. tuberculosis enzyme, an important drug target, complexed with the product UDP-GlcNAc (top: uridyltransferase active site) and with cacodylate anion (middle: on the crystallographic threefold axis). The acetyl-coA cofactor has been modelled in the acetyltransferase active site (bottom) (p. 275).

research papers

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The structures of the two alternatively spliced isoforms of human ketohexokinase, hepatic KHK-C and peripheral KHK-A, and of the ternary complex of KHK-A with the substrate fructose and AMP-PNP have been solved. The differences between KHK-A and KHK-C resulting from the spliced region are subtle and affect thermostability and probably flexibility; the mutations causing fructosuria were modelled.

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The structure of the DUF55 domain of human thymocyte nuclear protein 1, which was determined from partially tetartohedrally twinned crystals, is reported.

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The structure of the lysosomal 66.3 kDa protein, which crystallizes in the monoclinic space group C2, was solved by means of sulfur SAD phasing using data with an Ranom/Rp.i.m. ratio of 1.1.

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The crystal structures of DAPK–ADP–Mg2+ and DAPK–AMP-PNP–Mg2+ complexes were determined at 1.85 and 2.00 Å resolution, respectively. Comparison of the two nucleotide-bound states with apo DAPK revealed localized changes in the glycine-rich loop region that were indicative of a transition from a more open state to a more closed state on binding of the nucleotide substrate and to an intermediate state with the bound nucleotide product.

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A revised EDM–DEDM algorithm for phase refinement is described, together with its application to proteins, with special attention being given to molecular-replacement cases.

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The crystal structure of C2b has been determined at 1.8 Å resolution, which reveals the arrangement of its three complement control protein (CCP) modules. A model for complement component C2 is presented and its conformational changes during the C3-convertase formation are also discussed.

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The crystal structure of M. tuberculosis GlmU has been determined in an unliganded form and in complex with UDP-GlcNAc or GlcN-1-P. NMR-based enzymatic activity assays suggest that the presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity.

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Two single-crystal X-ray diffraction data sets for cyclosporine A were measured to high resolution using synchrotron radiation at temperatures of 5 and 90 K. They allowed an accurate determination of its molecular and electronic structure.

short communications

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The structure of uncomplexed plasmepsin II from P. falciparum is shown to contain noncoplanar catalytic aspartic acid residues.

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The representation of crystallographic model characteristics in the form of a polygon allows the quick comparison of a model with a set of previously solved structures.

addenda and errata

Acta Cryst. (2009). D65, 301
doi: 10.1107/S0907444909005824
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