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2bzd

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Galactose recognition by the carbohydrate-binding module of a bacterial sialidase.

Structural highlights

2bzd is a 3 chain structure with sequence from Micromonospora viridifaciens. This structure supersedes the now removed PDB entry 2bq9. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NANH_MICVI To release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Newstead SL, Watson JN, Bennet AJ, Taylor G. Galactose recognition by the carbohydrate-binding module of a bacterial sialidase. Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1483-91. Epub 2005, Oct 19. PMID:16239725 doi:10.1107/S0907444905026132

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2bzd"

Categories: Large Structures | Micromonospora viridifaciens | Newstead SL | Taylor G

@@ Line 3: / Line 3: @@
 <StructureSection load='2bzd' size='340' side='right'caption='[[2bzd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bzd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"micromonospora_viridifaciens"_routien "micromonospora viridifaciens" routien]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bq9 2bq9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BZD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bzd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Micromonospora_viridifaciens Micromonospora viridifaciens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2bq9 2bq9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BZD FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1eur|1eur]], [[1eus|1eus]], [[1eut|1eut]], [[1euu|1euu]], [[1w8n|1w8n]], [[1w8o|1w8o]], [[1wcq|1wcq]], [[2ber|2ber]], [[2bq9|2bq9]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bzd OCA], [https://pdbe.org/2bzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bzd RCSB], [https://www.ebi.ac.uk/pdbsum/2bzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bzd ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/NANH_MICVI NANH_MICVI]] To release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors.
+[https://www.uniprot.org/uniprot/NANH_MICVI NANH_MICVI] To release sialic acids for use as carbon and energy sources for this non-pathogenic bacterium while in pathogenic microorganisms, sialidases have been suggested to be pathogenic factors.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Micromonospora viridifaciens routien]]
-[[Category: Exo-alpha-sialidase]]
 [[Category: Large Structures]]
-[[Category: Newstead, S L]]
+[[Category: Micromonospora viridifaciens]]
-[[Category: Taylor, G]]
+[[Category: Newstead SL]]
-[[Category: Carbohydrate binding module]]
+[[Category: Taylor G]]
-[[Category: Glycosidase]]
-[[Category: Hydrolase]]
-[[Category: Sialidase]]

2bzd

From Proteopedia

Current revision

Galactose recognition by the carbohydrate-binding module of a bacterial sialidase.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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