1m4y
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1m4y.gif|left|200px]] | + | [[Image:1m4y.gif|left|200px]] |
| - | + | ||
| - | '''Crystal structure of HslV from Thermotoga maritima''' | + | {{Structure |
| + | |PDB= 1m4y |SIZE=350|CAPTION= <scene name='initialview01'>1m4y</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of HslV from Thermotoga maritima''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1M4Y is a [ | + | 1M4Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M4Y OCA]. |
==Reference== | ==Reference== | ||
| - | Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV., Song HK, Bochtler M, Azim MK, Hartmann C, Huber R, Ramachandran R, Biophys Chem. 2003;100(1-3):437-52. PMID:[http:// | + | Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV., Song HK, Bochtler M, Azim MK, Hartmann C, Huber R, Ramachandran R, Biophys Chem. 2003;100(1-3):437-52. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12646382 12646382] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| Line 22: | Line 31: | ||
[[Category: n-terminal catalytic threonine residue]] | [[Category: n-terminal catalytic threonine residue]] | ||
| - | ''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 12:39:00 2008'' |
Revision as of 10:39, 20 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of HslV from Thermotoga maritima
Overview
Heat-shock locus VU (HslVU) is an ATP-dependent proteolytic system and a prokaryotic homolog of the proteasome. It consists of HslV, the protease, and HslU, the ATPase and chaperone. We have cloned, sequenced and expressed both protein components from the hyperthermophile Thermotoga maritima. T. maritima HslU hydrolyzes a variety of nucleotides in a temperature-dependent manner, with the optimum lying between 75 and 80 degrees C. It is also nucleotide-unspecific for activation of HslV against amidolytic and caseinolytic activity. The Escherichia coli and T. maritima HslU proteins mutually stimulate HslV proteins from both sources, suggesting a conserved activation mechanism. The crystal structure of T. maritima HslV was determined and refined to 2.1-A resolution. The structure of the dodecameric enzyme is well conserved compared to those from E. coli and Haemophilus influenzae. A comparison of known HslV structures confirms the presence of a cation-binding site, although its exact role in the proteolytic mechanism of HslV remains unclear. Amongst factors responsible for the thermostability of T. maritima HslV, extensive ionic interactions/salt-bridge networks, which occur specifically in the T. maritima enzyme in comparison to its mesophilic counterparts, seem to play an important role.
About this Structure
1M4Y is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV., Song HK, Bochtler M, Azim MK, Hartmann C, Huber R, Ramachandran R, Biophys Chem. 2003;100(1-3):437-52. PMID:12646382
Page seeded by OCA on Thu Mar 20 12:39:00 2008
