1qno: Difference between revisions

Revision as of 15:41, 21 February 2008

THE 3-D STRUCTURE OF A TRICHODERMA REESEI B-MANNANASE FROM GLYCOSIDE HYDROLASE FAMILY 5

OverviewOverview

The crystal structure of the catalytic core domain of beta-mannanase from the fungus Trichoderma reesei has been determined at a resolution of 1.5 A. The structure was solved using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P2(1). The map computed with the experimental phases was enhanced by the application of an automated model building and refinement procedure using the amplitudes and experimental phases as observations. This approach is expected to be of more general application. The structure of the native enzyme and complexes with Tris-HCl and mannobiose are also reported: the mannobiose binds in subsites +1 and +2. The structure is briefly compared with that of the homologous beta-mannanase from the bacterium Thermomonospora fusca.

About this StructureAbout this Structure

1QNO is a Single protein structure of sequence from Hypocrea jecorina with and as ligands. Active as Mannan endo-1,4-beta-mannosidase, with EC number 3.2.1.78 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

The three-dimensional structure of a Trichoderma reesei beta-mannanase from glycoside hydrolase family 5., Sabini E, Schubert H, Murshudov G, Wilson KS, Siika-Aho M, Penttila M, Acta Crystallogr D Biol Crystallogr. 2000 Jan;56(Pt 1):3-13. PMID:10666621

Page seeded by OCA on Thu Feb 21 14:41:41 2008

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OCA

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 ==Overview==
-The crystal structure of the catalytic core domain of beta-mannanase from, the fungus Trichoderma reesei has been determined at a resolution of 1.5, A. The structure was solved using the anomalous scattering from a single, non-isomorphous platinum complex with two heavy-metal sites in space group, P2(1). The map computed with the experimental phases was enhanced by the, application of an automated model building and refinement procedure using, the amplitudes and experimental phases as observations. This approach is, expected to be of more general application. The structure of the native, enzyme and complexes with Tris-HCl and mannobiose are also reported: the, mannobiose binds in subsites +1 and +2. The structure is briefly compared, with that of the homologous beta-mannanase from the bacterium, Thermomonospora fusca.
+The crystal structure of the catalytic core domain of beta-mannanase from the fungus Trichoderma reesei has been determined at a resolution of 1.5 A. The structure was solved using the anomalous scattering from a single non-isomorphous platinum complex with two heavy-metal sites in space group P2(1). The map computed with the experimental phases was enhanced by the application of an automated model building and refinement procedure using the amplitudes and experimental phases as observations. This approach is expected to be of more general application. The structure of the native enzyme and complexes with Tris-HCl and mannobiose are also reported: the mannobiose binds in subsites +1 and +2. The structure is briefly compared with that of the homologous beta-mannanase from the bacterium Thermomonospora fusca.
 ==About this Structure==
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 [[Category: Schubert, H.]]
 [[Category: Siika-Aho, M.]]
-[[Category: Wilson, K.S.]]
+[[Category: Wilson, K S.]]
 [[Category: NAG]]
 [[Category: TRS]]
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 [[Category: trichoderma reesei]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:01:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:41 2008''