1m4y
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(New page: 200px<br /><applet load="1m4y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m4y, resolution 2.1Å" /> '''Crystal structure of ...)
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Revision as of 19:01, 20 November 2007
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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 with NA as ligand. 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
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