View source for 8or6


==Crystal structure of Drosophila melanogaster alpha-amylase==
<StructureSection load='8or6' size='340' side='right'caption='[[8or6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8or6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8OR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8OR6 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</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=8or6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8or6 OCA], [https://pdbe.org/8or6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8or6 RCSB], [https://www.ebi.ac.uk/pdbsum/8or6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8or6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMYA_DROME AMYA_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Insects rely on carbohydrates such as starch and glycogen as an energy supply for growth of larvae and for longevity. In this sense alpha-amylases have essential roles under extreme conditions, e.g., during nutritional or temperature stress, thereby contributing to survival of the insect. This makes them interesting targets for combating insect pests. Drosophila melanogaster alpha-amylase, DMA, which belongs to the glycoside hydrolase family 13, sub family 15, has been studied from an evolutionary, biochemical, and structural point of view. Our studies revealed that the DMA enzyme is active over a broad temperature and pH range, which is in agreement with the fluctuating environmental changes with which the insect is confronted. Crystal structures disclosed a new nearly fully solvated metal ion, only coordinated to the protein via Gln263. This residue is only conserved in the subgroup of D. melanogaster and may thus contribute to the enzyme adaptive response to large temperature variations. Studies of the effect of plant inhibitors and the pseudo-tetrasaccharide inhibitor acarbose on DMA activity, allowed us to underline the important role of the so-called flexible loop on activity/inhibition, but also to suggest that the inhibition modes of the wheat inhibitors WI-1 and WI-3 on DMA, are likely different.

Structural and Functional Characterization of Drosophila melanogaster alpha-Amylase.,Rhimi M, Da Lage JL, Haser R, Feller G, Aghajari N Molecules. 2023 Jul 11;28(14):5327. doi: 10.3390/molecules28145327. PMID:37513201<ref>PMID:37513201</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8or6" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Aghajari N]]
[[Category: Haser R]]