2bzd

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[[Image:2bzd.jpg|left|200px]]<br /><applet load="2bzd" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2bzd.jpg|left|200px]]
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caption="2bzd, resolution 2.00&Aring;" />
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'''GALACTOSE RECOGNITION BY THE CARBOHYDRATE-BINDING MODULE OF A BACTERIAL SIALIDASE.'''<br />
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{{Structure
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|PDB= 2bzd |SIZE=350|CAPTION= <scene name='initialview01'>2bzd</scene>, resolution 2.00&Aring;
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|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18]
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|GENE=
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}}
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'''GALACTOSE RECOGNITION BY THE CARBOHYDRATE-BINDING MODULE OF A BACTERIAL SIALIDASE.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BZD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Micromonospora_viridifaciens Micromonospora viridifaciens] with <scene name='pdbligand=GAL:'>GAL</scene>, <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 2BQ9. Active as [http://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] Known structural/functional Site: <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZD OCA].
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2BZD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Micromonospora_viridifaciens Micromonospora viridifaciens]. This structure supersedes the now removed PDB entry 2BQ9. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZD OCA].
==Reference==
==Reference==
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Galactose recognition by the carbohydrate-binding module of a bacterial sialidase., Newstead SL, Watson JN, Bennet AJ, Taylor G, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1483-91. Epub 2005, Oct 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16239725 16239725]
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Galactose recognition by the carbohydrate-binding module of a bacterial sialidase., Newstead SL, Watson JN, Bennet AJ, Taylor G, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1483-91. Epub 2005, Oct 19. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16239725 16239725]
[[Category: Exo-alpha-sialidase]]
[[Category: Exo-alpha-sialidase]]
[[Category: Micromonospora viridifaciens]]
[[Category: Micromonospora viridifaciens]]
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[[Category: sialidase]]
[[Category: sialidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:08:46 2008''

Revision as of 14:08, 20 March 2008


PDB ID 2bzd

Drag the structure with the mouse to rotate
, resolution 2.00Å
Sites:
Ligands: , and
Activity: Exo-alpha-sialidase, with EC number 3.2.1.18
Coordinates: save as pdb, mmCIF, xml



GALACTOSE RECOGNITION BY THE CARBOHYDRATE-BINDING MODULE OF A BACTERIAL SIALIDASE.


Overview

Glycoside hydrolases often possess carbohydrate-binding modules (CBMs) in addition to their catalytic domains, which help target the enzymes to appropriate substrates and thereby increase their catalytic efficiency. Sialidases hydrolyse the release of sialic acid from a variety of glycoconjugates and play significant roles in the pathogenesis of a number of important diseases. The sialidase from Micromonospora viridifaciens has a CBM which recognizes galactose. The CBM is linked to the catalytic domain by an immunoglobulin-like domain, resulting in the galactose binding site sitting above the catalytic site, suggesting an interplay between the two sites. By studying nine crystallographically independent structures of the M. viridifaciens sialidase, the relative flexibility of the three domains was analysed. A detailed study is also presented of the recognition of galactose and lactose by the M. viridifaciens CBM. The striking structure of this sialidase suggests a role for the CBM in binding to galactose residues unmasked by the adjacent catalytic site.

About this Structure

2BZD is a Single protein structure of sequence from Micromonospora viridifaciens. This structure supersedes the now removed PDB entry 2BQ9. Full crystallographic information is available from OCA.

Reference

Galactose recognition by the carbohydrate-binding module of a bacterial sialidase., Newstead SL, Watson JN, Bennet AJ, Taylor G, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1483-91. Epub 2005, Oct 19. PMID:16239725

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