1dys: Difference between revisions

Revision as of 13:22, 21 February 2008

ENDOGLUCANASE CEL6B FROM HUMICOLA INSOLENS

OverviewOverview

Cellulases are traditionally classified as either endoglucanases or cellobiohydrolases on the basis of their respective catalytic activities on crystalline cellulose, which is generally hydrolysed more efficiently only by the cellobiohydrolases. On the basis of the Trichoderma reesei cellobiohydrolase II structure, it was proposed that the active-site tunnel of cellobiohydrolases permitted the processive hydrolysis of cellulose, whereas the corresponding endoglucanases would display open active-site clefts [Rouvinen, Bergfors, Teeri, Knowles and Jones (1990) Science 249, 380-386]. Glycoside hydrolase family 6 contains both cellobiohydrolases and endoglucanases. The structure of the catalytic core of the family 6 endoglucanase Cel6B from Humicola insolens has been solved by molecular replacement with the known T. reesei cellobiohydrolase II as the search model. Strangely, at the sequence level, this enzyme exhibits the highest sequence similarity to family 6 cellobiohydrolases and displays just one of the loop deletions traditionally associated with endoglucanases in this family. However, this enzyme shows no activity on crystalline substrates but a high activity on soluble substrates, which is typical of an endoglucanase. The three-dimensional structure reveals that the deletion of just a single loop of the active site, coupled with the resultant conformational change in a second 'cellobiohydrolase-specific' loop, peels open the active-site tunnel to reveal a substrate-binding groove.

About this StructureAbout this Structure

1DYS is a Single protein structure of sequence from Humicola insolens. Active as Cellulase, with EC number 3.2.1.4 Known structural/functional Sites: and . Full crystallographic information is available from OCA.

ReferenceReference

Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution., Davies GJ, Brzozowski AM, Dauter M, Varrot A, Schulein M, Biochem J. 2000 May 15;348 Pt 1:201-7. PMID:10794732

Page seeded by OCA on Thu Feb 21 12:21:59 2008

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OCA

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 ==Overview==
-Cellulases are traditionally classified as either endoglucanases or, cellobiohydrolases on the basis of their respective catalytic activities, on crystalline cellulose, which is generally hydrolysed more efficiently, only by the cellobiohydrolases. On the basis of the Trichoderma reesei, cellobiohydrolase II structure, it was proposed that the active-site, tunnel of cellobiohydrolases permitted the processive hydrolysis of, cellulose, whereas the corresponding endoglucanases would display open, active-site clefts [Rouvinen, Bergfors, Teeri, Knowles and Jones (1990), Science 249, 380-386]. Glycoside hydrolase family 6 contains both, cellobiohydrolases and endoglucanases. The structure of the catalytic core, of the family 6 endoglucanase Cel6B from Humicola insolens has been solved, by molecular replacement with the known T. reesei cellobiohydrolase II as, the search model. Strangely, at the sequence level, this enzyme exhibits, the highest sequence similarity to family 6 cellobiohydrolases and, displays just one of the loop deletions traditionally associated with, endoglucanases in this family. However, this enzyme shows no activity on, crystalline substrates but a high activity on soluble substrates, which is, typical of an endoglucanase. The three-dimensional structure reveals that, the deletion of just a single loop of the active site, coupled with the, resultant conformational change in a second 'cellobiohydrolase-specific', loop, peels open the active-site tunnel to reveal a substrate-binding, groove.
+Cellulases are traditionally classified as either endoglucanases or cellobiohydrolases on the basis of their respective catalytic activities on crystalline cellulose, which is generally hydrolysed more efficiently only by the cellobiohydrolases. On the basis of the Trichoderma reesei cellobiohydrolase II structure, it was proposed that the active-site tunnel of cellobiohydrolases permitted the processive hydrolysis of cellulose, whereas the corresponding endoglucanases would display open active-site clefts [Rouvinen, Bergfors, Teeri, Knowles and Jones (1990) Science 249, 380-386]. Glycoside hydrolase family 6 contains both cellobiohydrolases and endoglucanases. The structure of the catalytic core of the family 6 endoglucanase Cel6B from Humicola insolens has been solved by molecular replacement with the known T. reesei cellobiohydrolase II as the search model. Strangely, at the sequence level, this enzyme exhibits the highest sequence similarity to family 6 cellobiohydrolases and displays just one of the loop deletions traditionally associated with endoglucanases in this family. However, this enzyme shows no activity on crystalline substrates but a high activity on soluble substrates, which is typical of an endoglucanase. The three-dimensional structure reveals that the deletion of just a single loop of the active site, coupled with the resultant conformational change in a second 'cellobiohydrolase-specific' loop, peels open the active-site tunnel to reveal a substrate-binding groove.
 ==About this Structure==
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 [[Category: Humicola insolens]]
 [[Category: Single protein]]
-[[Category: Brzozowski, A.M.]]
+[[Category: Brzozowski, A M.]]
 [[Category: Dauter, M.]]
-[[Category: Davies, G.J.]]
+[[Category: Davies, G J.]]
 [[Category: Schulein, M.]]
 [[Category: Varrot, A.]]
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 [[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:36:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:21:59 2008''