We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1a39

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1a39.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1a39.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1a39| PDB=1a39 | SCENE= }}
{{STRUCTURE_1a39| PDB=1a39 | SCENE= }}
-
'''HUMICOLA INSOLENS ENDOCELLULASE EGI S37W, P39W DOUBLE-MUTANT'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9335168}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9335168 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9335168}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Glycosylated protein]]
[[Category: Glycosylated protein]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:44:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:54:31 2008''

Revision as of 12:54, 30 June 2008

Image:1a39.png

Template:STRUCTURE 1a39

HUMICOLA INSOLENS ENDOCELLULASE EGI S37W, P39W DOUBLE-MUTANT

Template:ABSTRACT PUBMED 9335168

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

Page seeded by OCA on Mon Jun 30 15:54:31 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1a39"
Personal tools