2bzd: Difference between revisions
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<StructureSection load='2bzd' size='340' side='right'caption='[[2bzd]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2bzd' size='340' side='right'caption='[[2bzd]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2bzd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <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=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id=' | <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='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> | <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> | </table> | ||
== Function == | == 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. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Micromonospora viridifaciens]] | ||
[[Category: | [[Category: Newstead SL]] | ||
[[Category: | [[Category: Taylor G]] | ||
Latest revision as of 16:59, 13 December 2023
Galactose recognition by the carbohydrate-binding module of a bacterial sialidase.Galactose recognition by the carbohydrate-binding module of a bacterial sialidase.
Structural highlights
FunctionNANH_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 PubMedGlycoside 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. See AlsoReferences
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