View source for 5goq


==Crystal structure of alkaline invertase InvA from Anabaena sp. PCC 7120 complexed with glucose==
<StructureSection load='5goq' size='340' side='right'caption='[[5goq]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5goq]] 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=5GOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GOQ 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]] 2.75&#8491;</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=MSE:SELENOMETHIONINE'>MSE</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=5goq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5goq OCA], [https://pdbe.org/5goq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5goq RCSB], [https://www.ebi.ac.uk/pdbsum/5goq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5goq 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5goq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Invertase|Invertase]]
== References ==
<references/>
__TOC__
</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]]