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[[Image:1g0c.jpg|left|200px]]


{{Structure
==ALKALINE CELLULASE K CATALYTIC DOMAIN-CELLOBIOSE COMPLEX==
|PDB= 1g0c |SIZE=350|CAPTION= <scene name='initialview01'>1g0c</scene>, resolution 1.9&Aring;
<StructureSection load='1g0c' size='340' side='right'caption='[[1g0c]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=ACY:ACETIC ACID'>ACY</scene>
<table><tr><td colspan='2'>[[1g0c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._KSM-635 Bacillus sp. KSM-635]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G0C FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=PRD_900005:beta-cellobiose'>PRD_900005</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=1g0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0c OCA], [https://pdbe.org/1g0c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0c RCSB], [https://www.ebi.ac.uk/pdbsum/1g0c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0c ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GUN_BACS6 GUN_BACS6]
== 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/g0/1g0c_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=1g0c ConSurf].
<div style="clear:both"></div>


'''ALKALINE CELLULASE K CATALYTIC DOMAIN-CELLOBIOSE COMPLEX'''
==See Also==
 
*[[Glucanase 3D structures|Glucanase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The crystal structure of the catalytic domain of alkaline cellulase K was determined at 1.9 A resolution. Because of the most alkaliphilic nature and it's highest activity at pH 9.5, it is used commercially in laundry detergents. An analysis of the structural bases of the alkaliphilic character of the enzyme suggested a mechanism similar to that previously proposed for alkaline proteases, that is, an increase in the number of Arg, His, and Gln residues, and a decrease in Asp and Lys residues. Some ion pairs were formed by the gained Arg residues, which is similar to what has been found in the alkaline proteases. Lys-Asp ion pairs are disfavored and partly replaced with Arg-Asp ion pairs. The alkaline adaptation appeared to be a remodeling of ion pairs so that the charge balance is kept in the high pH range.
[[Category: Bacillus sp. KSM-635]]
 
[[Category: Large Structures]]
==About this Structure==
[[Category: Hakamada Y]]
1G0C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0C OCA].
[[Category: Ishida H]]
 
[[Category: Ito S]]
==Reference==
[[Category: Noda J]]
Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme., Shirai T, Ishida H, Noda J, Yamane T, Ozaki K, Hakamada Y, Ito S, J Mol Biol. 2001 Jul 27;310(5):1079-87. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11501997 11501997]
[[Category: Ozaki K]]
[[Category: Bacillus sp.]]
[[Category: Shirai T]]
[[Category: Cellulase]]
[[Category: Yamane T]]
[[Category: Single protein]]
[[Category: Hakamada, Y.]]
[[Category: Ishida, H.]]
[[Category: Ito, S.]]
[[Category: Noda, J.]]
[[Category: Ozaki, K.]]
[[Category: Shirai, T.]]
[[Category: Yamane, T.]]
[[Category: ACY]]
[[Category: CBI]]
[[Category: CD]]
[[Category: alpha/beta barrel]]
[[Category: cellobiose complex]]
[[Category: tim-barrel]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:23 2008''

Latest revision as of 13:23, 13 March 2024

ALKALINE CELLULASE K CATALYTIC DOMAIN-CELLOBIOSE COMPLEX

1g0c, resolution 1.90Å

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