1uv4

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[[Image:1uv4.gif|left|200px]]<br /><applet load="1uv4" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1uv4.gif|left|200px]]
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caption="1uv4, resolution 1.50&Aring;" />
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'''NATIVE BACILLUS SUBTILIS ARABINANASE ARB43A'''<br />
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{{Structure
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|PDB= 1uv4 |SIZE=350|CAPTION= <scene name='initialview01'>1uv4</scene>, resolution 1.50&Aring;
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|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99]
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|GENE=
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}}
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'''NATIVE BACILLUS SUBTILIS ARABINANASE ARB43A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1UV4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arabinan_endo-1,5-alpha-L-arabinosidase Arabinan endo-1,5-alpha-L-arabinosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.99 3.2.1.99] Known structural/functional Site: <scene name='pdbsite=AC1:Edo+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UV4 OCA].
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1UV4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UV4 OCA].
==Reference==
==Reference==
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Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A., Proctor MR, Taylor EJ, Nurizzo D, Turkenburg JP, Lloyd RM, Vardakou M, Davies GJ, Gilbert HJ, Proc Natl Acad Sci U S A. 2005 Feb 22;102(8):2697-702. Epub 2005 Feb 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15708971 15708971]
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Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A., Proctor MR, Taylor EJ, Nurizzo D, Turkenburg JP, Lloyd RM, Vardakou M, Davies GJ, Gilbert HJ, Proc Natl Acad Sci U S A. 2005 Feb 22;102(8):2697-702. Epub 2005 Feb 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15708971 15708971]
[[Category: Arabinan endo-1,5-alpha-L-arabinosidase]]
[[Category: Arabinan endo-1,5-alpha-L-arabinosidase]]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
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[[Category: hydrolase]]
[[Category: hydrolase]]
[[Category: propeller]]
[[Category: propeller]]
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[[Category: subtilis]]
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[[Category: subtili]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:28:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:37:10 2008''

Revision as of 12:37, 20 March 2008


PDB ID 1uv4

Drag the structure with the mouse to rotate
, resolution 1.50Å
Sites:
Ligands: and
Activity: Arabinan endo-1,5-alpha-L-arabinosidase, with EC number 3.2.1.99
Coordinates: save as pdb, mmCIF, xml



NATIVE BACILLUS SUBTILIS ARABINANASE ARB43A


Overview

Enzymes acting on polymeric substrates are frequently classified as exo or endo, reflecting their preference for, or ignorance of, polymer chain ends. Most biotechnological applications, especially in the field of polysaccharide degradation, require either endo- or exo-acting hydrolases, or they harness the essential synergy between these two modes of action. Here, we have used genomic data in tandem with structure to modify, radically, the chain-end specificity of the Cellvibrio japonicus exo-arabinanase CjArb43A. The structure of Bacillus subtilis endo-arabinanase 43A (BsArb43A) in harness with chain-end recognition kinetics of CjArb43A directed a rational design approach that led to the conversion of the Cellvibrio enzyme from an exo to an endo mode of action. One of the exo-acting mutants, D35L/Q316A, displays similar activity to WT CjArb43A and the removal of the steric block mediated by the side chains of Gln-316 and Asp-53 at the -3 subsite confers its capacity to attack internal glycoside bonds. This study provides a template for the production of tailored industrial catalysts. The introduction of subtle changes informed by comparative 3D structural and genomic data can lead to fundamental changes in the mode of action of these enzymes.

About this Structure

1UV4 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A., Proctor MR, Taylor EJ, Nurizzo D, Turkenburg JP, Lloyd RM, Vardakou M, Davies GJ, Gilbert HJ, Proc Natl Acad Sci U S A. 2005 Feb 22;102(8):2697-702. Epub 2005 Feb 11. PMID:15708971

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