2klm

Solution Structure of L11 with SAXS and RDC

spinqualitylabelsall models 2klm Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2klm is a 1 chain structure with sequence from Thermus thermophilus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Hybrid , Solution NMR , X-ray solution scattering Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL11_THET8 One of the L7 dimers in conjuction with L11 and its bound segment of 23S rRNA forms what is known as the L7/L12 stalk, which extends beyond the surface of the 70S ribosome. The stalk is preferentially stabilized in 70S versus 50S crystals.[HAMAP-Rule:MF_00736_B] This protein binds directly to 23S ribosomal RNA.[HAMAP-Rule:MF_00736_B] In the 70S ribosome is in a position where it could interact transiently with the A site tRNA during translation.[HAMAP-Rule:MF_00736_B] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Determining architectures of multicomponent proteins or protein complexes in solution is a challenging problem. Here we report a methodology that simultaneously uses residual dipolar couplings (RDC) and the small-angle X-ray scattering (SAXS) restraints to mutually orient subunits and define the global shape of multicomponent proteins and protein complexes. Our methodology is implemented in an efficient algorithm and demonstrated using five examples. First, we demonstrate the general approach with simulated data for the HIV-1 protease, a globular homodimeric protein. Second, we use experimental data to determine the structures of the two-domain proteins L11 and gammaD-Crystallin, in which the linkers between the domains are relatively rigid. Finally, complexes with K(d) values in the high micro- to millimolar range (weakly associating proteins), such as a homodimeric GB1 variant, and with K(d) values in the nanomolar range (tightly bound), such as the heterodimeric complex of the ILK ankyrin repeat domain (ARD) and PINCH LIM1 domain, respectively, are evaluated. Furthermore, the proteins or protein complexes that were determined using this method exhibit better solution structures than those obtained by either NMR or X-ray crystallography alone as judged based on the pair-distance distribution functions (PDDF) calculated from experimental SAXS data and back-calculated from the structures. Determination of multicomponent protein structures in solution using global orientation and shape restraints.,Wang J, Zuo X, Yu P, Byeon IJ, Jung J, Wang X, Dyba M, Seifert S, Schwieters CD, Qin J, Gronenborn AM, Wang YX J Am Chem Soc. 2009 Aug 5;131(30):10507-15. PMID:19722627 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein L11 3D structures

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