5z9t
From Proteopedia
(Difference between revisions)
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<StructureSection load='5z9t' size='340' side='right'caption='[[5z9t]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5z9t' size='340' side='right'caption='[[5z9t]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5z9t]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z9T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5z9t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"photobacter_splendidum"_(sic)_beijerinck_1900 "photobacter splendidum" (sic) beijerinck 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z9T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z9T 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>, <scene name='pdbligand=LGU:ALPHA-L-GULURONATE'>LGU</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LGU:ALPHA-L-GULURONATE'>LGU</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5z9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z9t OCA], [http://pdbe.org/5z9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z9t RCSB], [http://www.ebi.ac.uk/pdbsum/5z9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z9t ProSAT]</span></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=5z9t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z9t OCA], [http://pdbe.org/5z9t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z9t RCSB], [http://www.ebi.ac.uk/pdbsum/5z9t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z9t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Alginate lyases have a wide range of industrial applications, such as oligosaccharide preparation, medical treatment, and bioconversion. Therefore, the discovery and characterization of novel alginate lyases are extremely important. PL-6 alginate lyases are classified into two groups: those with a single domain or two domains. However, only one structure of a two-domain alginate lyase has been determined to date. In this study, we characterized a novel single-domain PL-6 alginate lyase (named AlyF). According to the biochemical analysis, AlyF possesses unique features compared with other PL-6 enzymes, including (1) a Ca(2+)-independent catalytic mechanism and (2) a PolyG-specific cleavage specificity that predominantly produces trisaccharides. The structures of AlyF and its complexes described here reveal the structural basis for these unique features and substrate binding mechanisms, which were further confirmed using mutagenesis. More importantly, we determined the possible subsites specifying the predominantly trisaccharide products of AlyF, which may facilitate the rational design of AlyF for potential applications in preparing a single alginate oligomer. | ||
| + | |||
| + | Structural insights into a novel Ca(2+)-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution.,Lyu Q, Zhang K, Shi Y, Li W, Diao X, Liu W Biochim Biophys Acta Gen Subj. 2019 Apr 17;1863(7):1167-1176. doi:, 10.1016/j.bbagen.2019.04.013. PMID:31004719<ref>PMID:31004719</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5z9t" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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[[Category: Li, Z J]] | [[Category: Li, Z J]] | ||
[[Category: Liu, W Z]] | [[Category: Liu, W Z]] | ||
| - | [[Category: | + | [[Category: Lyu, Q Q]] |
[[Category: Zhang, K K]] | [[Category: Zhang, K K]] | ||
[[Category: Compelx structure]] | [[Category: Compelx structure]] | ||
[[Category: Lyase]] | [[Category: Lyase]] | ||
Revision as of 09:03, 1 May 2019
a new PL6 alginate lyase complex with trisaccharide
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