1s2o

<table><tr><td colspan='2'>[[1s2o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aphanocapsa_sp._(strain_n-1) Aphanocapsa sp. (strain n-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2O OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1S2O FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">spp ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1148 Aphanocapsa sp. (strain N-1)])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sucrose-phosphate_phosphatase Sucrose-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.24 3.1.3.24] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1s2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2o OCA], [http://pdbe.org/1s2o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s2o RCSB], [http://www.ebi.ac.uk/pdbsum/1s2o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s2o ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Sucrose-phosphatase (SPP) catalyzes the final step in the pathway of sucrose biosynthesis in both plants and cyanobacteria, and the SPPs from these two groups of organisms are closely related. We have crystallized the enzyme from the cyanobacterium Synechocystis sp PCC 6803 and determined its crystal structure alone and in complex with various ligands. The protein consists of a core domain containing the catalytic site and a smaller cap domain that contains a glucose binding site. Two flexible hinge loops link the two domains, forming a structure that resembles a pair of sugar tongs. The glucose binding site plays a major role in determining the enzyme's remarkable substrate specificity and is also important for its inhibition by sucrose and glucose. It is proposed that the catalytic reaction is initiated by nucleophilic attack on the substrate by Asp9 and involves formation of a covalent phospho-Asp9-enzyme intermediate. From modeling based on the SPP structure, we predict that the noncatalytic SPP-like domain of the Synechocystis sucrose-phosphate synthase could bind sucrose-6(F)-phosphate and propose that this domain might be involved in metabolite channeling between the last two enzymes in the pathway of sucrose synthesis.

The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell.,Fieulaine S, Lunn JE, Borel F, Ferrer JL Plant Cell. 2005 Jul;17(7):2049-58. Epub 2005 Jun 3. PMID:15937230<ref>PMID:15937230</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1s2o" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Sucrose-phosphate phosphatase]]

[[Category: Borel, F]]

[[Category: Ferrer, J L]]

[[Category: Fieulaine, S]]

[[Category: Lunn, J E]]

[[Category: Sucrose]]