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==Crystal structure of alkaline invertase InvA from Anabaena sp. PCC 7120==
==Crystal structure of alkaline invertase InvA from Anabaena sp. PCC 7120==
<StructureSection load='5gor' size='340' side='right' caption='[[5gor]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
<StructureSection load='5gor' size='340' side='right'caption='[[5gor]], [[Resolution|resolution]] 2.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5gor]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GOR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GOR FirstGlance]. <br>
<table><tr><td colspan='2'>[[5gor]] is a 6 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=5GOR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GOR 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=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.673&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5goo|5goo]], [[5gop|5gop]], [[5goq|5goq]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gor OCA], [https://pdbe.org/5gor PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gor RCSB], [https://www.ebi.ac.uk/pdbsum/5gor PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gor 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=5gor FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gor OCA], [http://pdbe.org/5gor PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gor RCSB], [http://www.ebi.ac.uk/pdbsum/5gor PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gor ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8YWS9_NOSS1 Q8YWS9_NOSS1]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5gor" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5gor" style="background-color:#fffaf0;"></div>
==See Also==
*[[Invertase|Invertase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Beta-fructofuranosidase]]
[[Category: Large Structures]]
[[Category: Cai, K]]
[[Category: Nostoc sp. PCC 7120 = FACHB-418]]
[[Category: Chen, Y]]
[[Category: Cai K]]
[[Category: Hu, H X]]
[[Category: Chen Y]]
[[Category: Hu, P F]]
[[Category: Hu HX]]
[[Category: Jiang, Y L]]
[[Category: Hu PF]]
[[Category: Xie, J]]
[[Category: Jiang YL]]
[[Category: Yang, F]]
[[Category: Xie J]]
[[Category: Zhou, C Z]]
[[Category: Yang F]]
[[Category: Alkaline invertase]]
[[Category: Zhou CZ]]
[[Category: Cyanobacteria]]
[[Category: Glycoside hydrolase family 100]]
[[Category: Hydrolase]]
[[Category: Sucrose hydrolysis]]

Latest revision as of 14:38, 2 August 2023

Crystal structure of alkaline invertase InvA from Anabaena sp. PCC 7120Crystal structure of alkaline invertase InvA from Anabaena sp. PCC 7120

Structural highlights

5gor is a 6 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.673Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8YWS9_NOSS1

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Xie J, Cai K, Hu HX, Jiang YL, Yang F, Hu PF, Cao DD, Li WF, Chen Y, Zhou CZ. Structural Analysis of the Catalytic Mechanism and Substrate Specificity of Anabaena Alkaline Invertase InvA Reveals a Novel Glucosidase. J Biol Chem. 2016 Dec 2;291(49):25667-25677. Epub 2016 Oct 24. PMID:27777307 doi:http://dx.doi.org/10.1074/jbc.M116.759290

5gor, resolution 2.67Å

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