1mbx
From Proteopedia
(New page: 200px<br /><applet load="1mbx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mbx, resolution 2.25Å" /> '''CRYSTAL STRUCTURE AN...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1mbx.gif|left|200px]]<br /><applet load="1mbx" size=" | + | [[Image:1mbx.gif|left|200px]]<br /><applet load="1mbx" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mbx, resolution 2.25Å" /> | caption="1mbx, resolution 2.25Å" /> | ||
'''CRYSTAL STRUCTURE ANALYSIS OF ClpSN WITH TRANSITION METAL ION BOUND'''<br /> | '''CRYSTAL STRUCTURE ANALYSIS OF ClpSN WITH TRANSITION METAL ION BOUND'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Substrate selectivity and proteolytic activity for the E. coli | + | 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 Structure== | ==About this Structure== | ||
| - | 1MBX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL, ZN, YBT and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MBX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=YBT:'>YBT</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MBX OCA]. |
==Reference== | ==Reference== | ||
| Line 15: | Line 15: | ||
[[Category: Esser, L.]] | [[Category: Esser, L.]] | ||
[[Category: Guo, F.]] | [[Category: Guo, F.]] | ||
| - | [[Category: Maurizi, M | + | [[Category: Maurizi, M R.]] |
| - | [[Category: Singh, S | + | [[Category: Singh, S K.]] |
[[Category: Xia, D.]] | [[Category: Xia, D.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
| Line 28: | Line 28: | ||
[[Category: protein binding]] | [[Category: protein binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:53:39 2008'' |
Revision as of 11:53, 21 February 2008
|
CRYSTAL STRUCTURE ANALYSIS OF ClpSN WITH TRANSITION METAL ION BOUND
Overview
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 Structure
1MBX is a Protein complex structure of sequences from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.
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:12235156
Page seeded by OCA on Thu Feb 21 13:53:39 2008
Categories: Escherichia coli | Protein complex | Esser, L. | Guo, F. | Maurizi, M R. | Singh, S K. | Xia, D. | CL | GOL | YBT | ZN | Aaa+ family | Adaptors | Atp-dependent protease | Hsp100/clp chaperone | Protein binding
