5f7u
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5f7u is ON HOLD Authors: Light, S.H., Anderson, W.F., Center for Structural Genomics of Infectious Diseases (CSGID) Description: Cycloalternan-form...) |
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- | '''Unreleased structure''' | ||
- | + | ==Cycloalternan-forming enzyme from Listeria monocytogenes in complex with pentasaccharide substrate== | |
+ | <StructureSection load='5f7u' size='340' side='right'caption='[[5f7u]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[5f7u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F7U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F7U 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]] 1.7Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PRD_900001:alpha-maltose'>PRD_900001</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=5f7u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f7u OCA], [https://pdbe.org/5f7u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f7u RCSB], [https://www.ebi.ac.uk/pdbsum/5f7u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f7u ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q8Y4J2_LISMO Q8Y4J2_LISMO] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Here we employ a 'systems structural biology' approach to functionally characterize an unconventional alpha-glucan metabolic pathway from the food-borne pathogen Listeria monocytogenes (Lm). Crystal structure determination coupled with basic biochemical and biophysical assays allowed for the identification of anabolic, transport, catabolic and regulatory portions of the cycloalternan pathway. These findings provide numerous insights into cycloalternan pathway function and reveal the mechanism of repressor, open reading frame, kinase (ROK) transcription regulators. Moreover, by developing a structural overview we were able to anticipate the cycloalternan pathway's role in the metabolism of partially hydrolysed starch derivatives and demonstrate its involvement in Lm pathogenesis. These findings suggest that the cycloalternan pathway plays a role in interspecies resource competition-potentially within the host gastrointestinal tract-and establish the methodological framework for characterizing bacterial systems of unknown function. | ||
- | + | Structure to function of an alpha-glucan metabolic pathway that promotes Listeria monocytogenes pathogenesis.,Light SH, Cahoon LA, Halavaty AS, Freitag NE, Anderson WF Nat Microbiol. 2016 Nov 7;2:16202. doi: 10.1038/nmicrobiol.2016.202. PMID:27819654<ref>PMID:27819654</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | [[Category: | + | </div> |
- | [[Category: | + | <div class="pdbe-citations 5f7u" style="background-color:#fffaf0;"></div> |
- | [[Category: Anderson | + | == References == |
- | [[Category: | + | <references/> |
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Listeria monocytogenes EGD-e]] | ||
+ | [[Category: Anderson WF]] | ||
+ | [[Category: Light SH]] |
Current revision
Cycloalternan-forming enzyme from Listeria monocytogenes in complex with pentasaccharide substrate
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