1mbx
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CRYSTAL STRUCTURE ANALYSIS OF ClpSN WITH TRANSITION METAL ION BOUND
OverviewOverview
Substrate selectivity and proteolytic activity for the E. coli, ATP-dependent protease, ClpAP, is modulated by an adaptor protein, ClpS., ClpS binds to ClpA, the regulatory component of the ClpAP complex. We, report the crystal structure of ClpS in complex with the isolated, N-terminal domain of ClpA in two different crystal forms at 2.3- and 3.3-A, resolution. The ClpS structure forms an alpha/beta-sandwich and is, topologically analogous to the C-terminal domain of the ribosomal protein, L7/L12. ClpS contacts two surfaces on the N-terminal domain in both, crystal forms; the more extensive interface was shown to be favored in, solution by protease protection experiments. The N-terminal 20 residues of, ClpS are not visible in the crystal structures; the removal of the first, 17 residues produces ClpSDeltaN, which binds to the ClpA N-domain but no, longer inhibits ClpA activity. A zinc binding site involving two His and, one Glu residue was identified crystallographically in the N-terminal, domain of ClpA. In a model of ClpS bound to hexameric ClpA, ClpS is, oriented with its N terminus directed toward the distal surface of ClpA, suggesting that the N-terminal region of ClpS may affect productive, substrate interactions at the apical surface or substrate entry into the, ClpA translocation channel.
About this StructureAbout this Structure
1MBX is a Protein complex structure of sequences from Escherichia coli with CL, ZN, YBT and GOL as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA., Guo F, Esser L, Singh SK, Maurizi MR, Xia D, J Biol Chem. 2002 Nov 29;277(48):46753-62. Epub 2002 Sep 15. PMID:12235156
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