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7 citations found for Myers, J.
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Crystals of pectate lyase A from E. chrysanthemi, a plant virulence factor, have been obtained and shown to diffract to 2.4 Å.
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The title compound, C34H30N4O2, lies on an inversion center and consists of two 3-substituted-1H-indole units linked by a 1,2-dimethylenehydrazine bridge. It is one of numerous examples in which two aromatic ring systems are joined by this 4-atom bridge. The geometry of the centrosymmetric bridge is: C(arom)—C = 1.444 (3), C=N = 1.284 (3), N—N = 1.414 (4) Å, C(arom)—C=N = 122.6 (2) and C=N—N = 111.9 (2)°. The nine non-H atoms of the indole unit lie in a plane (δr.m.s. = 0.0089 Å) which is twisted 6.0 (2)° with respect to the hydrazine bridge plane. The benzyloxymethyl substituents do not lie in the plane of the rest of the molecule and are in a folded rather than an extended conformation. This is described by the three torsion angles in the middle of the C=N—C—O—CBz group, viz. 98.5 (3), −62.1 (3), and −66.3 (2)°.
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The structures of a six- and a seven-membered tellurium- and nitrogen-containing (Te—N) heterocycle represent the first structurally characterized members of their respective classes. When compared to their sulfur analogs, they exhibit slightly greater deviations from planarity to accommodate the larger chalcogenide atom. Intermolecular N—H
O hydrogen bonding forms centrosymmetric
(8) dimers in the six-membered hetereocyclic compound and chains in the seven-membered hetereocyclic compound, while intermolecular Te
O contacts exist in the former.
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Three structure determinations of Mycobacterium paratuberculosis and Burkholderia thailandensis IspD are reported (PDB entries 7kmw, 4zdq and 4ys8). In addition, the biophysical characterization of the enzymes and the binding affinity of the B. thailandensis enzyme in complex with cytidine triphosphate are reported.
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The crystal structure of the catalytic domain of MARK4 was determined and compared with those of other proteins belonging to the MARK/PAR-1 protein kinase family.