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4l9a
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal structure of Smu.1393c from cariogenic pathogen Streptococcus mutans== | |
| - | + | <StructureSection load='4l9a' size='340' side='right' caption='[[4l9a]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[4l9a]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_mutans_ua159 Streptococcus mutans ua159]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l80 3l80]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L9A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L9A FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMU_1393c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210007 Streptococcus mutans UA159])</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=4l9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l9a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l9a RCSB], [http://www.ebi.ac.uk/pdbsum/4l9a PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The protein Smu.1393c from Streptococcus mutans is annotated as a putative alpha/beta hydrolase, but it has low sequence identity to the structure-known alpha/beta hydrolases. Here we present the crystal structure of Smu.1393c at 2.0 A resolution. Smu.1393c has a fully open alkaline substrate pocket, whose conformation is unique among other similar hydrolase structures. Three residues, Ser101, His251, and Glu125, were identified as the active center of Smu.1393c. By screening a series of artificial hydrolase substrates, we demonstrated Smu.1393c had low carboxylesterase activity towards short-chain carboxyl esters, which provided a clue for exploring the in vivo function of Smu.1393c. Proteins 2013; (c) 2013 Wiley Periodicals, Inc. | ||
| - | + | Structural and functional characterization of a novel alpha/beta hydrolase from cariogenic pathogen Streptococcus mutans.,Wang Z, Li L, Su XD Proteins. 2013 Sep 30. doi: 10.1002/prot.24418. PMID:24115105<ref>PMID:24115105</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | + | </div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Streptococcus mutans ua159]] | [[Category: Streptococcus mutans ua159]] | ||
| - | [[Category: Li, L | + | [[Category: Li, L]] |
| - | [[Category: Su, X D | + | [[Category: Su, X D]] |
| - | [[Category: Wang, Z | + | [[Category: Wang, Z]] |
[[Category: Alpha/beta hydrolase]] | [[Category: Alpha/beta hydrolase]] | ||
[[Category: Carboxylesterase]] | [[Category: Carboxylesterase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 14:58, 21 December 2014
Crystal structure of Smu.1393c from cariogenic pathogen Streptococcus mutans
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