5z73

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'''Unreleased structure'''
 
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The entry 5z73 is ON HOLD until Paper Publication
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==Crystal structure of alkaline/neutral invertase InvB from Anabaena sp. PCC 7120==
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<StructureSection load='5z73' size='340' side='right' caption='[[5z73]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5z73]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z73 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z73 FirstGlance]. <br>
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</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>
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<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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-fructofuranosidase Beta-fructofuranosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.26 3.2.1.26] </span></td></tr>
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<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=5z73 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z73 OCA], [http://pdbe.org/5z73 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z73 RCSB], [http://www.ebi.ac.uk/pdbsum/5z73 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z73 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Anabaena sp. PCC 7120 encodes two alkaline/neutral invertases, namely InvA and InvB. Following our recently reported InvA structure, here we report the crystal structure of the heterocyst-specific InvB. Despite sharing an overall structure similar to InvA, InvB possesses a much higher catalytic activity. Structural comparisons of the catalytic pockets reveal that Arg430 of InvB adopts a different conformation, which may facilitate the deprotonation of the catalytic residue Glu415. We propose that the higher activity may be responsible for the vital role of InvB in heterocyst development and nitrogen fixation. Furthermore, phylogenetic analysis combined with activity assays also suggests the role of this highly conserved arginine in plants and cyanobacteria, as well as some proteobacteria living in highly extreme environments.
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Authors:
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Structural and enzymatic analyses of Anabaena heterocyst-specific alkaline invertase InvB.,Xie J, Hu HX, Cai K, Xia LY, Yang F, Jiang YL, Chen Y, Zhou CZ FEBS Lett. 2018 May;592(9):1589-1601. doi: 10.1002/1873-3468.13041. Epub 2018 Apr, 10. PMID:29578606<ref>PMID:29578606</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5z73" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Beta-fructofuranosidase]]
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[[Category: Cai, K]]
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[[Category: Chen, Y]]
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[[Category: Hu, H X]]
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[[Category: Jiang, Y L]]
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[[Category: Xie, J]]
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[[Category: Yang, F]]
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[[Category: Zhou, C Z]]
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[[Category: Alkaline/neutral invertase]]
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[[Category: Cyanobacteria]]
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[[Category: Glycoside hydrolase family 100]]
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[[Category: Hydrolase]]
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[[Category: Sucrose hydrolysis]]

Revision as of 05:29, 30 May 2018

Crystal structure of alkaline/neutral invertase InvB from Anabaena sp. PCC 7120

5z73, resolution 1.93Å

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