1m4y: Difference between revisions

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[[Image:1m4y.gif|left|200px]]


{{Structure
==Crystal structure of HslV from Thermotoga maritima==
|PDB= 1m4y |SIZE=350|CAPTION= <scene name='initialview01'>1m4y</scene>, resolution 2.1&Aring;
<StructureSection load='1m4y' size='340' side='right'caption='[[1m4y]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NA:SODIUM ION'>NA</scene>
<table><tr><td colspan='2'>[[1m4y]] is a 3 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M4Y FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m4y OCA], [https://pdbe.org/1m4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m4y RCSB], [https://www.ebi.ac.uk/pdbsum/1m4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m4y ProSAT]</span></td></tr>
 
</table>
'''Crystal structure of HslV from Thermotoga maritima'''
== Function ==
 
[https://www.uniprot.org/uniprot/HSLV_THEMA HSLV_THEMA] Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.<ref>PMID:12646382</ref>
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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.
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m4/1m4y_consurf.spt"</scriptWhenChecked>
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].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==Reference==
  </jmolCheckbox>
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]
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1m4y ConSurf].
[[Category: Single protein]]
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: Azim, M K.]]
[[Category: Azim MK]]
[[Category: Bochtler, M B.]]
[[Category: Bochtler MB]]
[[Category: Hartmann, C.]]
[[Category: Hartmann C]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Ramachandran, R.]]
[[Category: Ramachandran R]]
[[Category: Song, H K.]]
[[Category: Song HK]]
[[Category: NA]]
[[Category: n-terminal catalytic threonine residue]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:39:00 2008''

Latest revision as of 10:39, 14 February 2024

Crystal structure of HslV from Thermotoga maritimaCrystal structure of HslV from Thermotoga maritima

Structural highlights

1m4y is a 3 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HSLV_THEMA Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Song HK, Bochtler M, Azim MK, Hartmann C, Huber R, Ramachandran R. Isolation and characterization of the prokaryotic proteasome homolog HslVU (ClpQY) from Thermotoga maritima and the crystal structure of HslV. Biophys Chem. 2003;100(1-3):437-52. PMID:12646382

1m4y, resolution 2.10Å

Drag the structure with the mouse to rotate

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