1nlr
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1nlr.gif|left|200px]] | + | [[Image:1nlr.gif|left|200px]] |
| - | + | ||
| - | '''ENDO-1,4-BETA-GLUCANASE CELB2, CELLULASE, NATIVE STRUCTURE''' | + | {{Structure |
| + | |PDB= 1nlr |SIZE=350|CAPTION= <scene name='initialview01'>1nlr</scene>, resolution 1.75Å | ||
| + | |SITE= <scene name='pdbsite=GAB:General+Acid+Base'>GAB</scene> and <scene name='pdbsite=NF:Nucleophile+Site+Site_identifier+Gab+Site_description+Ge+...'>NF</scene> | ||
| + | |LIGAND= | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ENDO-1,4-BETA-GLUCANASE CELB2, CELLULASE, NATIVE STRUCTURE''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1NLR is a [ | + | 1NLR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLR OCA]. |
==Reference== | ==Reference== | ||
| - | The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution., Sulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ, Biochemistry. 1997 Dec 23;36(51):16032-9. PMID:[http:// | + | The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution., Sulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ, Biochemistry. 1997 Dec 23;36(51):16032-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9440876 9440876] |
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| Line 22: | Line 31: | ||
[[Category: glycosyl hydrolase]] | [[Category: glycosyl hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:58:28 2008'' |
Revision as of 10:58, 20 March 2008
| |||||||
| , resolution 1.75Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Activity: | Cellulase, with EC number 3.2.1.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ENDO-1,4-BETA-GLUCANASE CELB2, CELLULASE, NATIVE STRUCTURE
Overview
Cellulases are the glycoside hydrolases responsible for the enzymatic breakdown of the structural plant polymer cellulose. Together with xylanases they counteract the lmitless accumulation of plant biomass in nature and are of considerable fundamental and biotechnological interest. Endoglucanase CelB from Streptomyces lividans performs hydrolysis of the beta-1,4-glycosidic bonds of cellulose, with net retention of anomeric configuration. The enzyme is a member of glycoside hydrolase family 12 [Henrissat, B., and Bairoch, A. (1996) Biochem. J. 316, 695-696], which had previously eluded detailed structural analysis. A truncated, but cataytically competent form of CelB, locking the flexible linker region and cellulose-binding domain, has been constructed and overexpressed in a S. lividans expression system. The three-dimensional X-ray structure of the resulting catalytic domain, CelB2, has been solved by conventional multiple isomorphous replacement methods and refined to an R factor of 0.187 at 1.75 A resolution. The overall fold of the enzyme shows a remarkable similarity to that of family 11 xylanases, as previously predicted by hydrophobic clustering analysis [Torronen, A., Kubicek, C.P., and Henrissat, B. (1993) FEBS Lett. 321, 135-139]. The 23 kDa protein presents a jelly-roll topology, built up mainly by antiparallel beta-sheets arranged in a sandwich-like manner. A deep substrate-binding cleft runs across the surface, as has been observed in other endoglucanase structures, and is potentially able to accommodate up to five binding subsites. The likely catalytic nucleophile and Bronsted acid/base, residues Glu 120 and Glue 203, respectively, have their carboxylate groups separated by a distance of approximately 7.0 A and are located approximately 15 A from one end of the cleft, implying a -3 to +2 active site.
About this Structure
1NLR is a Single protein structure of sequence from Streptomyces lividans. Full crystallographic information is available from OCA.
Reference
The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution., Sulzenbacher G, Shareck F, Morosoli R, Dupont C, Davies GJ, Biochemistry. 1997 Dec 23;36(51):16032-9. PMID:9440876
Page seeded by OCA on Thu Mar 20 12:58:28 2008
