9buj
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of PfPL1 from Pseudoalteromonas fuliginea== | |
| + | <StructureSection load='9buj' size='340' side='right'caption='[[9buj]], [[Resolution|resolution]] 2.19Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9buj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudoalteromonas_fuliginea Pseudoalteromonas fuliginea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BUJ FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=9buj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9buj OCA], [https://pdbe.org/9buj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9buj RCSB], [https://www.ebi.ac.uk/pdbsum/9buj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9buj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A833EL34_9GAMM A0A833EL34_9GAMM] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pseudoalteromonas fuliginea sp. PS47 is a recently identified marine bacterium that has extensive enzymatic machinery to metabolize polysaccharides, including a locus that targets pectin-like substrates. This locus contains a gene (locus tag EU509_03255) that encodes a pectin-degrading lyase, called PfPL1, that belongs to polysaccharide lyase family 1 (PL1). The 2.2 A resolution X-ray crystal structure of PfPL1 reveals the compact parallel beta-helix fold of the PL1 family. The back side of the core parallel beta-helix opposite to the active site is a meandering set of five alpha-helices joined by lengthy loops. A comparison of the active site with those of other PL1 enzymes suggests a catalytic mechanism that is independent of metal ions, such as Ca(2+), but that substrate recognition may require metal ions. Overall, this work provides the first structural insight into a pectinase of marine origin and the first structure of a PL1 enzyme in subfamily 2. | ||
| - | + | The structure of a pectin-active family 1 polysaccharide lyase from the marine bacterium Pseudoalteromonas fuliginea.,Hobbs JK, Boraston AB Acta Crystallogr F Struct Biol Commun. 2024 Jul 1;80(Pt 7):142-147. doi: , 10.1107/S2053230X2400596X. Epub 2024 Jun 27. PMID:38935515<ref>PMID:38935515</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9buj" style="background-color:#fffaf0;"></div> |
| - | [[Category: Boraston | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudoalteromonas fuliginea]] | ||
| + | [[Category: Boraston AB]] | ||
| + | [[Category: Hobbs JK]] | ||
Current revision
Structure of PfPL1 from Pseudoalteromonas fuliginea
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