1a39

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[[Image:1a39.jpg|left|200px]]<br /><applet load="1a39" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1a39.jpg|left|200px]]
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caption="1a39, resolution 2.2&Aring;" />
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'''HUMICOLA INSOLENS ENDOCELLULASE EGI S37W, P39W DOUBLE-MUTANT'''<br />
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{{Structure
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|PDB= 1a39 |SIZE=350|CAPTION= <scene name='initialview01'>1a39</scene>, resolution 2.2&Aring;
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|SITE= <scene name='pdbsite=ACI:Catalytic+Acid/Base'>ACI</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile+As+Identified+By+2-Fluorocellobios+...'>NUC</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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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|GENE= POTENTIAL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=34413 Humicola insolens])
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}}
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'''HUMICOLA INSOLENS ENDOCELLULASE EGI S37W, P39W DOUBLE-MUTANT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1A39 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Known structural/functional Sites: <scene name='pdbsite=ACI:Catalytic+Acid/Base'>ACI</scene> and <scene name='pdbsite=NUC:Catalytic+Nucleophile+As+Identified+By+2-Fluorocellobios+...'>NUC</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A39 OCA].
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1A39 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Humicola_insolens Humicola insolens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A39 OCA].
==Reference==
==Reference==
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Oligosaccharide specificity of a family 7 endoglucanase: insertion of potential sugar-binding subsites., Davies GJ, Ducros V, Lewis RJ, Borchert TV, Schulein M, J Biotechnol. 1997 Sep 16;57(1-3):91-100. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9335168 9335168]
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Oligosaccharide specificity of a family 7 endoglucanase: insertion of potential sugar-binding subsites., Davies GJ, Ducros V, Lewis RJ, Borchert TV, Schulein M, J Biotechnol. 1997 Sep 16;57(1-3):91-100. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9335168 9335168]
[[Category: Cellulase]]
[[Category: Cellulase]]
[[Category: Humicola insolens]]
[[Category: Humicola insolens]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:52:13 2008''

Revision as of 07:52, 20 March 2008


PDB ID 1a39

Drag the structure with the mouse to rotate
, resolution 2.2Å
Sites: and
Ligands:
Gene: POTENTIAL (Humicola insolens)
Activity: Cellulase, with EC number 3.2.1.4
Coordinates: save as pdb, mmCIF, xml



HUMICOLA INSOLENS ENDOCELLULASE EGI S37W, P39W DOUBLE-MUTANT


Overview

Family 7 of the glycosyl hydrolases contains both endoglucanases and cellobiohydrolases. In addition to their different catalytic activities on crystalline substrates, the cellobiohydrolases differ from the endoglucanases in their activity on longer soluble substrates, indicative of a greater number of subsites on the enzyme. A double mutant (S37W, P39W) of the Humicola insolens endoglucanase I (EG I) has been constructed in order to mimic aspects of the subsite structure of the corresponding family 7 cellobiohydrolase, cellobiohydrolase-I (CBH I). The 3-D crystal structure of the double mutant has been solved and refined to a crystallographic R-factor of 0.17 at a resolution of 2.2 A (1 A = 0.1 nm). The two mutant tryptophans are clearly visible in the electron density and are in the same orientation as those found in the substrate binding groove of CBH I. In addition to the substitutions, the C-terminal amino acids (399QELQ), disordered in the native enzyme structure, are clearly visible and there are a small number of minor loop movements associated with differences in crystal packing. Kinetic determinations show that the S37W, P39W mutant EG I has almost identical activity, compared to native EG I, on small soluble cellodextrins. On phosphoric acid swollen cellulose there is a small (30%), but significant, decrease in the apparent KM indicating that the double mutant may indeed exhibit stronger binding to longer polymeric substrates.

About this Structure

1A39 is a Single protein structure of sequence from Humicola insolens. Full crystallographic information is available from OCA.

Reference

Oligosaccharide specificity of a family 7 endoglucanase: insertion of potential sugar-binding subsites., Davies GJ, Ducros V, Lewis RJ, Borchert TV, Schulein M, J Biotechnol. 1997 Sep 16;57(1-3):91-100. PMID:9335168

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