4hz8: Difference between revisions
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[[ | ==Crystal structure of BglB with natural substrate== | ||
<StructureSection load='4hz8' size='340' side='right' caption='[[4hz8]], [[Resolution|resolution]] 1.14Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4hz8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3fj0 3fj0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HZ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HZ8 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4hz6|4hz6]], [[4hz7|4hz7]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bglA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=77133 uncultured bacterium])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hz8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hz8 RCSB], [http://www.ebi.ac.uk/pdbsum/4hz8 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Beta-glucosidase enzymes (EC 3.2.1-3.2.3) hydrolyze sugars and are implicated in a wide spectrum of biological processes. Recently, we reported that beta-glucosidase has varied kinetic parameters for the natural and synthetic substrates [K.H Nam, S.J. Kim, M.Y. Kim, J.H. Kim, T.S. Yeo, C.M. Lee, H.K Jun, K.Y. Hwang. Crystal structure of engineered beta-glucosidase from a soil metagenome, Proteins 73 (2008) 788-793]. However, an understanding of the kinetic values of beta-glucosidase has not yet enabled the elucidation of its molecular function. Here, we report the X-ray crystal structure of beta-glucosidase with a glucose and cellobiose fragment from uncultured soil metagenome. From the various crystals, we obtained the pre-reaction (native), intermediate (disaccharide cleavage) and post-reaction (glucose binding) states of the active site pocket. These structures provide snapshots of the catalytic processing of beta-glucosidase. In addition, the intermediate state of the crystal structure provides insight into the substrate specificity of beta-glucosidase. These structural studies will facilitate elucidation of the architectural mechanism responsible for the substrate recognition of beta-glucosidase. | |||
Structural insights into the substrate recognition properties of beta-glucosidase.,Nam KH, Sung MW, Hwang KY Biochem Biophys Res Commun. 2010 Jan 1;391(1):1131-5. doi:, 10.1016/j.bbrc.2009.12.038. Epub 2009 Dec 11. PMID:20005197<ref>PMID:20005197</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Beta-glucosidase|Beta-glucosidase]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Uncultured bacterium]] | [[Category: Uncultured bacterium]] | ||
[[Category: Hwang, K Y | [[Category: Hwang, K Y]] | ||
[[Category: Nam, K H | [[Category: Nam, K H]] | ||
[[Category: Beta-glucosidase]] | [[Category: Beta-glucosidase]] | ||
[[Category: Bgl]] | [[Category: Bgl]] | ||
Revision as of 19:49, 10 December 2014
Crystal structure of BglB with natural substrateCrystal structure of BglB with natural substrate
Structural highlights
Publication Abstract from PubMedBeta-glucosidase enzymes (EC 3.2.1-3.2.3) hydrolyze sugars and are implicated in a wide spectrum of biological processes. Recently, we reported that beta-glucosidase has varied kinetic parameters for the natural and synthetic substrates [K.H Nam, S.J. Kim, M.Y. Kim, J.H. Kim, T.S. Yeo, C.M. Lee, H.K Jun, K.Y. Hwang. Crystal structure of engineered beta-glucosidase from a soil metagenome, Proteins 73 (2008) 788-793]. However, an understanding of the kinetic values of beta-glucosidase has not yet enabled the elucidation of its molecular function. Here, we report the X-ray crystal structure of beta-glucosidase with a glucose and cellobiose fragment from uncultured soil metagenome. From the various crystals, we obtained the pre-reaction (native), intermediate (disaccharide cleavage) and post-reaction (glucose binding) states of the active site pocket. These structures provide snapshots of the catalytic processing of beta-glucosidase. In addition, the intermediate state of the crystal structure provides insight into the substrate specificity of beta-glucosidase. These structural studies will facilitate elucidation of the architectural mechanism responsible for the substrate recognition of beta-glucosidase. Structural insights into the substrate recognition properties of beta-glucosidase.,Nam KH, Sung MW, Hwang KY Biochem Biophys Res Commun. 2010 Jan 1;391(1):1131-5. doi:, 10.1016/j.bbrc.2009.12.038. Epub 2009 Dec 11. PMID:20005197[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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