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Although Km varies ∼1000-fold ∼1000-foldcacrossthe molaccasesbasis of substhete binding is poorly understood.
Despite the wealth of biochemical/mechanistic data generated for UGM, the structural basis of substrate binding is still lacking.
Here the native FamD1 structure and three protein-ligand complexes are analyzed to investigate the molecular basis of substrate binding and catalysis.
The molecular basis of substrate binding and trade-offs is described further below (see also Figure 2 and Figure 2 figure supplement 1).
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The definition of unique patterns of amino acids in each group provides a rational basis for the classification of existing small molecule groups and provides a basis for prediction of substrate binding resides in novel ELKs.
On the basis of the present findings, we propose the following model of substrate binding of PahZ1KP-2 (Figure 5).
Mayer, M. P. et al. Multistep mechanism of substrate binding determines chaperone activity of Hsp70.
This suggests that TRiC employs different methods of substrate binding and folding.
Zhu, X. et al. Structural analysis of substrate binding by the molecular chaperone DnaK.
In its ATP-bound state, DnaK shows low affinity for substrates; however, the ADP-bound state has high substrate affinity and hence exhibits slow rates of substrate binding and release.
Lee, S., Choi, J. M. & Tsai, F. T. Visualizing the ATPase cycle in a protein disaggregating machine: structural basis for substrate binding by ClpB.
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