1um8
From Proteopedia
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| - | [[Image:1um8.jpg|left|200px]] | + | [[Image:1um8.jpg|left|200px]] |
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| - | '''Crystal structure of helicobacter pylori ClpX''' | + | {{Structure |
| + | |PDB= 1um8 |SIZE=350|CAPTION= <scene name='initialview01'>1um8</scene>, resolution 2.6Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= CLPX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Helicobacter pylori 26695]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of helicobacter pylori ClpX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UM8 is a [ | + | 1UM8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UM8 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of ClpX molecular chaperone from Helicobacter pylori., Kim DY, Kim KK, J Biol Chem. 2003 Dec 12;278(50):50664-70. Epub 2003 Sep 26. PMID:[http:// | + | Crystal structure of ClpX molecular chaperone from Helicobacter pylori., Kim DY, Kim KK, J Biol Chem. 2003 Dec 12;278(50):50664-70. Epub 2003 Sep 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14514695 14514695] |
[[Category: Helicobacter pylori 26695]] | [[Category: Helicobacter pylori 26695]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: clpp binding loop]] | [[Category: clpp binding loop]] | ||
| - | ''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 14:33:50 2008'' |
Revision as of 12:33, 20 March 2008
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| , resolution 2.6Å | |||||||
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| Ligands: | |||||||
| Gene: | CLPX (Helicobacter pylori 26695) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of helicobacter pylori ClpX
Overview
ClpX, a heat shock protein 100 chaperone, which acts as the regulatory subunit of the ATP-dependent ClpXP protease, is responsible for intracellular protein remodeling and degradation. To provide a structural basis for a better understanding of the function of the Clp ATPase family, the crystal structures of Helicobacter pylori ClpX, lacking an N-terminal Cys cluster region complexed with ADP, was determined. The overall structure of ClpX is similar to that of heat shock locus U (HslU), consisting of two subdomains, with ADP bound at the subdomain interface. The crystal structure of ClpX reveals that a conserved tripeptide (LGF) is located on the tip of ClpP binding loop extending from the N-terminal subdomain. A hexameric model of ClpX suggests that six tripeptides make hydrophobic contacts with the hydrophobic clefts of the ClpP heptmer asymmetrically. In addition, the nucleotide binding environment provides the structural explanation for the hexameric assembly and the modulation of ATPase activity.
About this Structure
1UM8 is a Single protein structure of sequence from Helicobacter pylori 26695. Full crystallographic information is available from OCA.
Reference
Crystal structure of ClpX molecular chaperone from Helicobacter pylori., Kim DY, Kim KK, J Biol Chem. 2003 Dec 12;278(50):50664-70. Epub 2003 Sep 26. PMID:14514695
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