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[[Image:1mee.gif|left|200px]]<br /><applet load="1mee" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mee, resolution 2.0&Aring;" />
'''THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C'''<br />


==Overview==
==THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C==
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 load='1mee' size='340' side='right'caption='[[1mee]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>


==About this Structure==
==See Also==
1MEE is a [http://en.wikipedia.org/wiki/Protein_complex 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] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEE OCA].
*[[Eglin|Eglin]]
 
*[[Subtilisin 3D structures|Subtilisin 3D structures]]
==Reference==
__TOC__
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=1793542 1793542]
</StructureSection>
[[Category: Bacillus pumilus]]
[[Category: Bacillus pumilus]]
[[Category: Hirudo medicinalis]]
[[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 Feb 21 13:54:24 2008''

Latest revision as of 10:43, 14 February 2024

THE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-CTHE COMPLEX BETWEEN THE SUBTILISIN FROM A MESOPHILIC BACTERIUM AND THE LEECH INHIBITOR EGLIN-C

Structural highlights

1mee is a 2 chain structure with sequence from Bacillus pumilus and Hirudo medicinalis. 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

SUBT_BACPU Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.

Evolutionary Conservation

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

See Also

1mee, resolution 2.00Å

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