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.

1mve

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mve.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1mve.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mve| PDB=1mve | SCENE= }}
{{STRUCTURE_1mve| PDB=1mve | SCENE= }}
-
'''Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes'''
+
===Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes===
-
==Overview==
+
<!--
-
The 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes (Fsbeta-glucanase) is classified as one of the family 16 glycosyl hydrolases. It hydrolyzes the glycosidic bond in the mixed-linked glucans containing beta-1,3- and beta-1,4-glycosidic linkages. We constructed a truncated form of recombinant Fsbeta-glucanase containing the catalytic domain from amino acid residues 1-258, which exhibited a higher thermal stability and enzymatic activity than the full-length enzyme. The crystal structure of the truncated Fsbeta-glucanase was solved at a resolution of 1.7A by the multiple wavelength anomalous dispersion (MAD) method using the anomalous signals from the seleno-methionine-labeled protein. The overall topology of the truncated Fsbeta-glucanase consists mainly of two eight-stranded anti-parallel beta-sheets arranged in a jellyroll beta-sandwich, similar to the fold of many glycosyl hydrolases and carbohydrate-binding modules. Sequence comparison with other bacterial glucanases showed that Fsbeta-glucanase is the only naturally occurring circularly permuted beta-glucanase with reversed sequences. Structural comparison shows that the engineered circular-permuted Bacillus enzymes are more similar to their parent enzymes with which they share approximately 70% sequence identity, than to the naturally occurring Fsbeta-glucanase of similar topology with 30% identity. This result suggests that protein structure relies more on sequence identity than topology. The high-resolution structure of Fsbeta-glucanase provides a structural rationale for the different activities obtained from a series of mutant glucanases and a basis for the development of engineered enzymes with increased activity and structural stability.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12842475}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12842475 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12842475}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Yuan, H S.]]
[[Category: Yuan, H S.]]
[[Category: Circular-permutated jellyroll protein]]
[[Category: Circular-permutated jellyroll protein]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:45:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:48:41 2008''

Revision as of 13:48, 28 July 2008

Image:1mve.png

Template:STRUCTURE 1mve

Crystal structure of a natural circularly-permutated jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes

Template:ABSTRACT PUBMED 12842475

About this Structure

1MVE is a Single protein structure of sequence from Fibrobacter succinogenes. Full crystallographic information is available from OCA.

Reference

Crystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes., Tsai LC, Shyur LF, Lee SH, Lin SS, Yuan HS, J Mol Biol. 2003 Jul 11;330(3):607-20. PMID:12842475

Page seeded by OCA on Mon Jul 28 16:48:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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