1kfg: Difference between revisions
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|PDB= 1kfg |SIZE=350|CAPTION= <scene name='initialview01'>1kfg</scene>, resolution 1.90Å | |PDB= 1kfg |SIZE=350|CAPTION= <scene name='initialview01'>1kfg</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=GS1:1-THIO-BETA-D-GLUCOPYRANOSE'>GS1</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SGC:4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE'>SGC</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene> | ||
|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]) | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1g87|1G87]], [[1ga7|1GA7]], [[1k72|1K72]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfg OCA], [http://www.ebi.ac.uk/pdbsum/1kfg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kfg RCSB]</span> | |||
}} | }} | ||
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[[Category: Haser, R.]] | [[Category: Haser, R.]] | ||
[[Category: Mandelman, D.]] | [[Category: Mandelman, D.]] | ||
[[Category: (alpha-alpha)6-barrel]] | [[Category: (alpha-alpha)6-barrel]] | ||
[[Category: cellulose binding domain]] | [[Category: cellulose binding domain]] | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:47:50 2008'' | ||
Revision as of 18:47, 30 March 2008
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| 1kfg, resolution 1.90Å | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | CA, GLC, GOL, GS1, MG, NI, SGC, TRS | ||||||||||||
| Gene: | CELCCG (Clostridium cellulolyticum) | ||||||||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||||||||
| Related: | 1G87, 1GA7, 1K72
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
The X-ray Crystal Structure of Cel9G from Clostridium cellulolyticum complexed with a Thio-Oligosaccharide Inhibitor
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
1KFG 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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