3ai7

<StructureSection load='3ai7' size='340' side='right' caption='[[3ai7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>

<table><tr><td colspan='2'>[[3ai7]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/As_1.2186 As 1.2186]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AI7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AI7 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fructose-6-phosphate_phosphoketolase Fructose-6-phosphate phosphoketolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.22 4.1.2.22] </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=3ai7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ai7 OCA], [http://pdbe.org/3ai7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ai7 RCSB], [http://www.ebi.ac.uk/pdbsum/3ai7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ai7 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The crystal structure of Bifidobacterium longum phosphoketolase, a thiamine diphosphate (TPP) dependent enzyme, has been determined at 2.2A resolution. The enzyme is a dimer with the active sites located at the interface between the two identical subunits with molecular mass of 92.5kDa. The bound TPP is almost completely shielded from solvent except for the catalytically important C2-carbon of the thiazolium ring, which can be accessed by a substrate sugar through a narrow funnel-shaped channel. In silico docking studies of B. longum phosphoketolase with its substrate enable us to propose a model for substrate binding. STRUCTURED SUMMARY: MINT-7985878: PKT (uniprotkb:Q6R2Q7) and PKT (uniprotkb:Q6R2Q7) bind (MI:0407) by X-ray crystallography (MI:0114).

Crystal structure of Bifidobacterium Longum phosphoketolase; key enzyme for glucose metabolism in Bifidobacterium.,Takahashi K, Tagami U, Shimba N, Kashiwagi T, Ishikawa K, Suzuki EI FEBS Lett. 2010 Aug 3. PMID:20674574<ref>PMID:20674574</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 3ai7" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: As 1 2186]]

[[Category: Fructose-6-phosphate phosphoketolase]]

[[Category: Ishikawa, K]]

[[Category: Kashiwagi, T]]

[[Category: Shimba, N]]

[[Category: Suzuki, E]]

[[Category: Tagami, U]]

[[Category: Takahashi, K]]

[[Category: Thiamine-diphosphate protein]]