1fjo: Difference between revisions

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[[Image:1fjo.jpg|left|200px]]


{{Structure
==THERMOLYSIN (60% ACETONE SOAKED CRYSTALS)==
|PDB= 1fjo |SIZE=350|CAPTION= <scene name='initialview01'>1fjo</scene>, resolution 2.0&Aring;
<StructureSection load='1fjo' size='340' side='right'caption='[[1fjo]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene> and <scene name='pdbligand=ACN:ACETONE'>ACN</scene>
<table><tr><td colspan='2'>[[1fjo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FJO FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Thermolysin Thermolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.27 3.4.24.27]  
</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&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACN:ACETONE'>ACN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1fjo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjo OCA], [https://pdbe.org/1fjo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fjo RCSB], [https://www.ebi.ac.uk/pdbsum/1fjo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fjo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/THER_BACTH THER_BACTH] Extracellular zinc metalloprotease.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fj/1fjo_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1fjo ConSurf].
<div style="clear:both"></div>


'''THERMOLYSIN (60% ACETONE SOAKED CRYSTALS)'''
==See Also==
 
*[[Thermolysin 3D structures|Thermolysin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Multiple Solvent Crystal Structures (MSCS) is a crystallographic technique to identify energetically favorable positions and orientations of small organic molecules on the surface of proteins. We determined the high-resolution crystal structures of thermolysin (TLN), generated from crystals soaked in 50--70% acetone, 50--80% acetonitrile and 50 mM phenol. The structures of the protein in the aqueous-organic mixtures are essentially the same as the native enzyme and a number of solvent interaction sites were identified. The distribution of probe molecules shows clusters in the main specificity pocket of the active site and a buried subsite. Within the active site, we compared the experimentally determined solvent positions with predictions from two computational functional group mapping techniques, GRID and Multiple Copy Simultaneous Search (MCSS). The experimentally determined small molecule positions are consistent with the structures of known protein--ligand complexes of TLN.
 
==About this Structure==
1FJO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thermoproteolyticus Bacillus thermoproteolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJO OCA].
 
==Reference==
Experimental and computational mapping of the binding surface of a crystalline protein., English AC, Groom CR, Hubbard RE, Protein Eng. 2001 Jan;14(1):47-59. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11287678 11287678]
[[Category: Bacillus thermoproteolyticus]]
[[Category: Bacillus thermoproteolyticus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Thermolysin]]
[[Category: English AC]]
[[Category: English, A C.]]
[[Category: Groom CR]]
[[Category: Groom, C R.]]
[[Category: Hubbard RE]]
[[Category: Hubbard, R E.]]
[[Category: ACN]]
[[Category: CA]]
[[Category: DMS]]
[[Category: ZN]]
[[Category: metalloproteinase]]
[[Category: organic solvent]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:09:59 2008''

Latest revision as of 10:15, 7 February 2024

THERMOLYSIN (60% ACETONE SOAKED CRYSTALS)THERMOLYSIN (60% ACETONE SOAKED CRYSTALS)

Structural highlights

1fjo is a 1 chain structure with sequence from Bacillus thermoproteolyticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

THER_BACTH Extracellular zinc metalloprotease.

Evolutionary Conservation

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

See Also

1fjo, resolution 2.00Å

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