View source for 6gne


==Catalytic domain of Starch Synthase IV from Arabidopsis thaliana bound to ADP and acarbose==
<StructureSection load='6gne' size='340' side='right' caption='[[6gne]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6gne]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GNE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACR:ALPHA-ACARBOSE'>ACR</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SS4, At4g18240, T9A21.90 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Starch_synthase Starch synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.21 2.4.1.21] </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=6gne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gne OCA], [http://pdbe.org/6gne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gne RCSB], [http://www.ebi.ac.uk/pdbsum/6gne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gne ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/SSY4_ARATH SSY4_ARATH]] Probably involved in the priming of starch granule formation. May play a regulatory role in the control of starch accumulation in plastids. Is necessary and sufficient to establish the correct number of starch granules observed in chloroplasts.<ref>PMID:17217470</ref> <ref>PMID:19666739</ref> <ref>PMID:21645200</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Starch synthases (SSs) are responsible for depositing the majority of glucoses in starch. Structural knowledge on these enzymes that is available from the crystal structures of rice granule bound starch synthase (GBSS) and barley SSI provides incomplete information on substrate binding and active site architecture. Here we report the crystal structures of the catalytic domains of SSIV from Arabidopsis thaliana, of GBSS from the cyanobacterium CLg1 and GBSSI from the glaucophyte Cyanophora paradoxa, with all three bound to ADP and the inhibitor acarbose. The SSIV structure illustrates in detail the modes of binding for both donor and acceptor in a plant SS. CLg1GBSS contains, in the same crystal structure, examples of molecules with and without bound acceptor, which illustrates the conformational changes induced upon acceptor binding that presumably precede catalytic activity. With structures available from several isoforms of plant and non-plant SSs, as well as the closely related bacterial glycogen synthases, we analyze, at the structural level, the common elements that define a SS, the elements that are necessary for substrate binding and singularities of the GBSS family that could underlie its processivity. While the phylogeny of the SSIII/IV/V has been recently discussed, we now further report the detailed evolutionary history of the GBSS/SSI/SSII type of SSs enlightening the origin of the GBSS enzymes used in our structural analysis.

Crystal Structures of the Catalytic Domain of Arabidopsis thaliana Starch Synthase IV, of Granule Bound Starch Synthase From CLg1 and of Granule Bound Starch Synthase I of Cyanophora paradoxa Illustrate Substrate Recognition in Starch Synthases.,Nielsen MM, Ruzanski C, Krucewicz K, Striebeck A, Cenci U, Ball SG, Palcic MM, Cuesta-Seijo JA Front Plant Sci. 2018 Aug 3;9:1138. doi: 10.3389/fpls.2018.01138. eCollection, 2018. PMID:30123236<ref>PMID:30123236</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6gne" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arath]]
[[Category: Starch synthase]]
[[Category: Cuesta-Seijo, J A]]
[[Category: Krucewicz, K]]
[[Category: Palcic, M M]]
[[Category: Ruzanski, C]]
[[Category: Striebeck, A]]
[[Category: Acarbose]]
[[Category: Adp]]
[[Category: Glycosyl transferase]]
[[Category: Transferase]]