1g0c: Difference between revisions

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New page: left|200px<br /><applet load="1g0c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g0c, resolution 1.9Å" /> '''ALKALINE CELLULASE K ...
 
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[[Image:1g0c.jpg|left|200px]]<br /><applet load="1g0c" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1g0c, resolution 1.9&Aring;" />
'''ALKALINE CELLULASE K CATALYTIC DOMAIN-CELLOBIOSE COMPLEX'''<br />


==Overview==
==ALKALINE CELLULASE K CATALYTIC DOMAIN-CELLOBIOSE COMPLEX==
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.
<StructureSection load='1g0c' size='340' side='right'caption='[[1g0c]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>


==About this Structure==
==See Also==
1G0C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with CBI, CD and ACY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G0C OCA].
*[[Glucanase 3D structures|Glucanase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11501997 11501997]
[[Category: Bacillus sp. KSM-635]]
[[Category: Bacillus sp.]]
[[Category: Large Structures]]
[[Category: Cellulase]]
[[Category: Hakamada Y]]
[[Category: Single protein]]
[[Category: Ishida H]]
[[Category: Hakamada, Y.]]
[[Category: Ito S]]
[[Category: Ishida, H.]]
[[Category: Noda J]]
[[Category: Ito, S.]]
[[Category: Ozaki K]]
[[Category: Noda, J.]]
[[Category: Shirai T]]
[[Category: Ozaki, K.]]
[[Category: Yamane T]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:34:53 2007''

Latest revision as of 13:23, 13 March 2024

ALKALINE CELLULASE K CATALYTIC DOMAIN-CELLOBIOSE COMPLEX

1g0c, resolution 1.90Å

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