1mbu: Difference between revisions
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[[Image:1mbu.jpg|left|200px]] | [[Image:1mbu.jpg|left|200px]] | ||
'''Crystal Structure Analysis of ClpSN heterodimer''' | {{Structure | ||
|PDB= 1mbu |SIZE=350|CAPTION= <scene name='initialview01'>1mbu</scene>, resolution 2.30Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=YBT:BIS-(2-HYDROXYETHYL)AMINO-TRIS(HYDROXYMETHYL)METHANE+YTTRIUM'>YBT</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal Structure Analysis of ClpSN heterodimer''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MBU is a [ | 1MBU is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBU OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12235156 12235156] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein binding]] | [[Category: protein binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:34 2008'' |
Revision as of 13:41, 20 March 2008
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, resolution 2.30Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
Crystal Structure Analysis of ClpSN heterodimer
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
1MBU is a Protein complex structure of sequences from Escherichia coli. 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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