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[[ | ==Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc== | ||
<StructureSection load='3sut' size='340' side='right' caption='[[3sut]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3sut]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Paenibacillus Paenibacillus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3SUT FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OAN:O-(2-ACETAMIDO-2-DEOXY+D-GLUCOPYRANOSYLIDENE)+AMINO-N-PHENYLCARBAMATE'>OAN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3sur|3sur]], [[3sus|3sus]], [[3suu|3suu]], [[3suv|3suv]], [[3suw|3suw]]</td></tr> | |||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Hex1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44249 Paenibacillus])</td></tr> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3sut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3sut RCSB], [http://www.ebi.ac.uk/pdbsum/3sut PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
One useful methodology that has been used to give insight into how chemically synthesized inhibitors bind to enzymes and the reasons underlying their potency is crystallographic studies of inhibitor-enzyme complexes. Presented here is the X-ray structural analysis of a representative family 20 exo-beta-N-acetylhexosaminidase in complex with various known classes of inhibitor of these types of enzymes, which highlights how different inhibitor classes can inhibit the same enzyme. This study will aid in the future development of inhibitors of not only exo-beta-N-acetylhexosaminidases but also other types of glycoside hydrolases. | |||
Gaining insight into the inhibition of glycoside hydrolase family 20 exo-beta-N-acetylhexosaminidases using a structural approach.,Sumida T, Stubbs KA, Ito M, Yokoyama S Org Biomol Chem. 2012 Apr 7;10(13):2607-12. Epub 2012 Feb 27. PMID:22367352<ref>PMID:22367352</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Beta-Hexosaminidase|Beta-Hexosaminidase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Beta-N-acetylhexosaminidase]] | [[Category: Beta-N-acetylhexosaminidase]] | ||
[[Category: Paenibacillus]] | [[Category: Paenibacillus]] | ||
Revision as of 08:29, 5 June 2014
Crystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAcCrystal structure of beta-hexosaminidase from Paenibacillus sp. TS12 in complex with PUGNAc
Structural highlights
Publication Abstract from PubMedOne useful methodology that has been used to give insight into how chemically synthesized inhibitors bind to enzymes and the reasons underlying their potency is crystallographic studies of inhibitor-enzyme complexes. Presented here is the X-ray structural analysis of a representative family 20 exo-beta-N-acetylhexosaminidase in complex with various known classes of inhibitor of these types of enzymes, which highlights how different inhibitor classes can inhibit the same enzyme. This study will aid in the future development of inhibitors of not only exo-beta-N-acetylhexosaminidases but also other types of glycoside hydrolases. Gaining insight into the inhibition of glycoside hydrolase family 20 exo-beta-N-acetylhexosaminidases using a structural approach.,Sumida T, Stubbs KA, Ito M, Yokoyama S Org Biomol Chem. 2012 Apr 7;10(13):2607-12. Epub 2012 Feb 27. PMID:22367352[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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