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1k72

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|PDB= 1k72 |SIZE=350|CAPTION= <scene name='initialview01'>1k72</scene>, resolution 1.80&Aring;
|PDB= 1k72 |SIZE=350|CAPTION= <scene name='initialview01'>1k72</scene>, resolution 1.80&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CBI:CELLOBIOSE'>CBI</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SCH:S-METHYL+THIOCYSTEINE+GROUP'>SCH</scene>
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|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]
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|ACTIVITY= <span class='plainlinks'>[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] </span>
|GENE= CelCCG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1521 Clostridium cellulolyticum])
|GENE= CelCCG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1521 Clostridium cellulolyticum])
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|DOMAIN=
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|RELATEDENTRY=[[1g87|1G87]], [[1ga2|1GA2]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k72 OCA], [http://www.ebi.ac.uk/pdbsum/1k72 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1k72 RCSB]</span>
}}
}}
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[[Category: Haser, R.]]
[[Category: Haser, R.]]
[[Category: Mandelman, D.]]
[[Category: Mandelman, D.]]
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[[Category: CA]]
 
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[[Category: CBI]]
 
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[[Category: GLC]]
 
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[[Category: GOL]]
 
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[[Category: MG]]
 
[[Category: (alpha-alpha)6-barrel]]
[[Category: (alpha-alpha)6-barrel]]
[[Category: cellotriose]]
[[Category: cellotriose]]
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[[Category: x-ray diffraction]]
[[Category: x-ray diffraction]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:13:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:44:20 2008''

Revision as of 18:44, 30 March 2008


PDB ID 1k72

Drag the structure with the mouse to rotate
, resolution 1.80Å
Ligands: , , , , ,
Gene: CelCCG (Clostridium cellulolyticum)
Activity: Cellulase, with EC number 3.2.1.4
Related: 1G87, 1GA2


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



The X-ray Crystal Structure Of Cel9G Complexed With cellotriose


Overview

Complete cellulose degradation is the first step in the use of biomass as a source of renewable energy. To this end, the engineering of novel cellulase activity, the activity responsible for the hydrolysis of the beta-1,4-glycosidic bonds in cellulose, is a topic of great interest. The high-resolution X-ray crystal structure of a multidomain endoglucanase from Clostridium cellulolyticum has been determined at a 1.6-A resolution. The endoglucanase, Cel9G, is comprised of a family 9 catalytic domain attached to a family III(c) cellulose-binding domain. The two domains together form a flat platform onto which crystalline cellulose is suggested to bind and be fed into the active-site cleft for endolytic hydrolysis. To further dissect the structural basis of cellulose binding and hydrolysis, the structures of Cel9G in the presence of cellobiose, cellotriose, and a DP-10 thio-oligosaccharide inhibitor were resolved at resolutions of 1.7, 1.8, and 1.9 A, respectively.

About this Structure

1K72 is a Single protein structure of sequence from Clostridium cellulolyticum. Full crystallographic information is available from OCA.

Reference

X-Ray crystal structure of the multidomain endoglucanase Cel9G from Clostridium cellulolyticum complexed with natural and synthetic cello-oligosaccharides., Mandelman D, Belaich A, Belaich JP, Aghajari N, Driguez H, Haser R, J Bacteriol. 2003 Jul;185(14):4127-35. PMID:12837787

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