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==Crystal structure of alkaline invertase InvA from Anabaena sp. PCC 7120 complexed with sucrose== | |||
<StructureSection load='5gop' size='340' side='right'caption='[[5gop]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5gop]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GOP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GOP 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]] 2.35Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PRD_900003:sucrose'>PRD_900003</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=5gop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gop OCA], [https://pdbe.org/5gop PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gop RCSB], [https://www.ebi.ac.uk/pdbsum/5gop PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gop ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8YWS9_NOSS1 Q8YWS9_NOSS1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Invertases catalyze the hydrolysis of sucrose to glucose and fructose, thereby playing a key role in primary metabolism and plant development. According to the optimum pH, invertases are classified into acid invertases (Ac-Invs) and alkaline/neutral invertases (A/N-Invs), which share no sequence homology. Compared with Ac-Invs that have been extensively studied, the structure and catalytic mechanism of A/N-Invs remain unknown. Here we report the crystal structures of Anabaena alkaline invertase InvA, which was proposed to be the ancestor of modern plant A/N-Invs. These structures are the first in the GH100 family. InvA exists as a hexamer in both crystal and solution. Each subunit consists of an (alpha/alpha)6 barrel core structure in addition to an insertion of three helices. A couple of structures in complex with the substrate or products enabled us to assign the subsites -1 and +1 specifically binding glucose and fructose, respectively. Structural comparison combined with enzymatic assays indicated that Asp-188 and Glu-414 are putative catalytic residues. Further analysis of the substrate binding pocket demonstrated that InvA possesses a stringent substrate specificity toward the alpha1,2-glycosidic bond of sucrose. Together, we suggest that InvA and homologs represent a novel family of glucosidases. | |||
Structural Analysis of the Catalytic Mechanism and Substrate Specificity of Anabaena Alkaline Invertase InvA Reveals a Novel Glucosidase.,Xie J, Cai K, Hu HX, Jiang YL, Yang F, Hu PF, Cao DD, Li WF, Chen Y, Zhou CZ J Biol Chem. 2016 Dec 2;291(49):25667-25677. Epub 2016 Oct 24. PMID:27777307<ref>PMID:27777307</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5gop" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Hu | *[[Invertase|Invertase]] | ||
[[Category: Hu | == References == | ||
[[Category: Jiang | <references/> | ||
[[Category: Xie | __TOC__ | ||
[[Category: Yang | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Nostoc sp. PCC 7120 = FACHB-418]] | |||
[[Category: Cai K]] | |||
[[Category: Chen Y]] | |||
[[Category: Hu HX]] | |||
[[Category: Hu PF]] | |||
[[Category: Jiang YL]] | |||
[[Category: Xie J]] | |||
[[Category: Yang F]] | |||
[[Category: Zhou CZ]] | |||
Latest revision as of 14:38, 2 August 2023
Crystal structure of alkaline invertase InvA from Anabaena sp. PCC 7120 complexed with sucroseCrystal structure of alkaline invertase InvA from Anabaena sp. PCC 7120 complexed with sucrose
Structural highlights
FunctionPublication Abstract from PubMedInvertases catalyze the hydrolysis of sucrose to glucose and fructose, thereby playing a key role in primary metabolism and plant development. According to the optimum pH, invertases are classified into acid invertases (Ac-Invs) and alkaline/neutral invertases (A/N-Invs), which share no sequence homology. Compared with Ac-Invs that have been extensively studied, the structure and catalytic mechanism of A/N-Invs remain unknown. Here we report the crystal structures of Anabaena alkaline invertase InvA, which was proposed to be the ancestor of modern plant A/N-Invs. These structures are the first in the GH100 family. InvA exists as a hexamer in both crystal and solution. Each subunit consists of an (alpha/alpha)6 barrel core structure in addition to an insertion of three helices. A couple of structures in complex with the substrate or products enabled us to assign the subsites -1 and +1 specifically binding glucose and fructose, respectively. Structural comparison combined with enzymatic assays indicated that Asp-188 and Glu-414 are putative catalytic residues. Further analysis of the substrate binding pocket demonstrated that InvA possesses a stringent substrate specificity toward the alpha1,2-glycosidic bond of sucrose. Together, we suggest that InvA and homologs represent a novel family of glucosidases. Structural Analysis of the Catalytic Mechanism and Substrate Specificity of Anabaena Alkaline Invertase InvA Reveals a Novel Glucosidase.,Xie J, Cai K, Hu HX, Jiang YL, Yang F, Hu PF, Cao DD, Li WF, Chen Y, Zhou CZ J Biol Chem. 2016 Dec 2;291(49):25667-25677. Epub 2016 Oct 24. PMID:27777307[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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