1gbg

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{{STRUCTURE_1gbg| PDB=1gbg | SCENE= }}
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'''BACILLUS LICHENIFORMIS BETA-GLUCANASE'''
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===BACILLUS LICHENIFORMIS BETA-GLUCANASE===
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==Overview==
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The crystal structure of the 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 A and refined to R = 16.5%. The protein has a similar beta-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-beta-D-glucan 4-glucanohydrolases.
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(as it appears on PubMed at http://www.pubmed.gov), where 7589539 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7589539}}
==About this Structure==
==About this Structure==
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[[Category: Hahn, M.]]
[[Category: Hahn, M.]]
[[Category: Heinemann, U.]]
[[Category: Heinemann, U.]]
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Revision as of 02:02, 1 July 2008

Template:STRUCTURE 1gbg

BACILLUS LICHENIFORMIS BETA-GLUCANASE

Template:ABSTRACT PUBMED 7589539

About this Structure

1GBG is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.

Reference

Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution., Hahn M, Pons J, Planas A, Querol E, Heinemann U, FEBS Lett. 1995 Oct 30;374(2):221-4. PMID:7589539

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