Dynamic Characteristics Analysis of a Rigid Body System with Spatial Multi-Point Supports

This paper presents the dynamic characteristics analysis of a rigid body system with spatial multi-point elastic supports, as well as the sensitivity analysis of support parameters. A rigid object is characterized by six degrees-of-freedom (DOFs) motions and considering the spatial location vector decomposition of elastic supports, a rigid body system dynamic model with spatial multi-point elastic supports is derived via the Lagrangian energy method. The system modal frequencies are calculated, and to be verified by finite element modal analysis results. Next, based on the above-mentioned model, system modal frequencies are obtained under different support locations, where the support stiffness components are different. Interpolate the stiffness components corresponding to each support location, calculate system modal frequencies, and the response surface model (RSM) for system modal frequencies is established. Further, based on the RSM modal analysis results, the allowable support location for the system modal insensitive area can be obtained. At last, a lubricating oil-tank system with four supports is taken as an example, and the effects of support spatial locations and stiffness components on the system inherent characteristics are discussed. This present work can provide a basis for the dynamic design of the spatial location and stiffness for this type of installation structures.

Structural insights as to how iron-loaded siderophores are imported into Mycobacterium tuberculosis by IrtAB

The ATP-binding cassette (ABC) transporter, IrtAB, plays a vital role in the replication and viability of Mycobacterium tuberculosis (Mtb), where its function is to import iron-loaded siderophores. Unusually, it adopts the typical fold of canonical ABC exporters. Here, we report the structure of unliganded Mtb IrtAB and its structure in complex with ATP, ADP, and an ATP analogue (AMP-PNP) at resolutions from 2.9 to 3.5 Å. In the ATP-bound state, the two nucleotide-binding domains (NBDs) form a "head-to-tail" dimer, but IrtAB has an unexpectedly occluded conformation, with the inner core forming a large hydrophilic cavity of about 4600 Å3. Comparison of the structure of the transporter in inward-facing and occluded conformations reveals that the NBD and the intracellular helical region of transmembrane domain (TMD) have an asymmetric allosteric mechanism when ATP binding/hydrolysis such that the one exhibits rigid-body rotation and the other moves in a concerted response as a rigid body. This study provides a molecular basis for the ATP-driven conformational changes that occur in IrtAB and an explanation as to how iron-loaded siderophores are imported into Mtb by IrtAB.