1mee: Difference between revisions

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-[[Image:1mee.gif|left|200px]]
- {{Structure
+==THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C==
-|PDB= 1mee |SIZE=350|CAPTION= <scene name='initialview01'>1mee</scene>, resolution 2.0&Aring;
+<StructureSection load='1mee' size='340' side='right'caption='[[1mee]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
+<table><tr><td colspan='2'>[[1mee]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus] and [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MEE FirstGlance]. <br>
-|ACTIVITY= [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62]
+</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=CA:CALCIUM+ION'>CA</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=1mee FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mee OCA], [https://pdbe.org/1mee PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mee RCSB], [https://www.ebi.ac.uk/pdbsum/1mee PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mee ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SUBT_BACPU SUBT_BACPU] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
+== 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/me/1mee_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=1mee ConSurf].
+<div style="clear:both"></div>
-'''THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C'''
+==See Also==
+*[[Eglin|Eglin]]
+*[[Subtilisin 3D structures|Subtilisin 3D structures]]
-==Overview==
+__TOC__
-The alkaline proteinase from the mesophilic bacterium Bacillus mesentericus has been crystallized in a 1:1 complex with the inhibitor eglin-C from the medical leech. The crystals have cell dimensions of a = 43.0, b = 71.9, c = 48.3 A and beta = 110.0 degrees and are in the space group P2(1). Three-dimensional data to 2.0 A have been recorded on film from a single crystal. The orientation and position of the complex in the unit cell have been established using the refined coordinates of subtilisin Carlsberg and of eglin-C as independent models. The structure of the complex has been refined by restrained least-squares minimization. The crystallographic R factor (= sigma[magnitude of Fo - magnitude of Fc[/sigma magnitude of Fo) is 15.1% including two Ca2+ ions and 312 water molecules. The structure is discussed in terms of its physicochemical properties in solution and its relation to other Bacillus subtilisins.
+</StructureSection>
-==About this Structure==
-MEE is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus] and [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEE OCA].
-==Reference==
-Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C., Dauter Z, Betzel C, Genov N, Pipon N, Wilson KS, Acta Crystallogr B. 1991 Oct 1;47 ( Pt 5):707-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1793542 1793542]
 [[Category: Bacillus pumilus]]
 [[Category: Hirudo medicinalis]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Subtilisin]]
+[[Category: Betzel C]]
-[[Category: Betzel, C.]]
+[[Category: Dauter Z]]
-[[Category: Dauter, Z.]]
+[[Category: Wilson KS]]
-[[Category: Wilson, K S.]]
-[[Category: CA]]
-[[Category: complex(serine proteinase-inhibitor)]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:42:27 2008''