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4ffi

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==Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose==
==Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose==
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<StructureSection load='4ffi' size='340' side='right' caption='[[4ffi]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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<StructureSection load='4ffi' size='340' side='right'caption='[[4ffi]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ffi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arthrobacter_ureafaciens Arthrobacter ureafaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FFI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ffi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Paenarthrobacter_ureafaciens Paenarthrobacter ureafaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FFI FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0UB:BETA-D-FRUCTOFURANOSYL-(2- 6)-BETA-D-FRUCTOFURANOSYL-(2- 6)-BETA-D-FRUCTOFURANOSE'>0UB</scene>, <scene name='pdbligand=LBS:6-O-BETA-D-FRUCTOFURANOSYL-BETA-D-FRUCTOFURANOSE'>LBS</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ffg|4ffg]], [[4ffh|4ffh]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FRU:FRUCTOSE'>FRU</scene>, <scene name='pdbligand=PRD_900051:levanbiose'>PRD_900051</scene>, <scene name='pdbligand=PRD_900063:levantriose'>PRD_900063</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lftA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=37931 Arthrobacter ureafaciens])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ffi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffi OCA], [https://pdbe.org/4ffi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ffi RCSB], [https://www.ebi.ac.uk/pdbsum/4ffi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ffi ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Levan_fructotransferase_(DFA-IV-forming) Levan fructotransferase (DFA-IV-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.16 4.2.2.16] </span></td></tr>
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</table>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ffi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ffi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ffi RCSB], [http://www.ebi.ac.uk/pdbsum/4ffi PDBsum]</span></td></tr>
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== Function ==
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<table>
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[https://www.uniprot.org/uniprot/Q9KJD0_FLASK Q9KJD0_FLASK]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Levan is beta-2,6-linked polymeric fructose and serves as reserve carbohydrate in some plants and microorganisms. Mobilization of fructose is usually mediated by enzymes such as glycoside hydrolase (GH), typically releasing a monosaccharide as a product. The enzyme levan fructotransferase (LFTase) of the GH32 family catalyzes an intramolecular fructosyl transfer reaction and results in production of cyclic difructose dianhydride, thus exhibiting a novel substrate-specificity. The mechanism by which LFTase carries out these functions via the structural fold conserved in the GH32 family is unknown. Here, we report the crystal structure of LFTase from Arthrobacter ureafaciens in apo form, as well as in complexes with sucrose and levanbiose, a difructosacchride with a beta-2,6-glycosidic linkage. Despite the similarity of its two-domain structure to members of the GH32 family, LFTase contains an active site that accommodates a difructosaccharide using the -1 and -2 subsites. This feature is unique among GH32 proteins and is facilitated by small side-chain residues in the loop region of a catalytic beta-propeller N-domain, which is conserved in the LFTase family. An additional oligosaccharide binding site was also characterized in the beta-sandwich C-domain, supporting its role in carbohydrate recognition. Together with functional analysis, our data provide a molecular basis for the catalytic mechanism of LFTase and suggest functional variations from other GH32 family proteins, notwithstanding the conserved structural elements.
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Structural and functional basis for substrate specificity and catalysis of levan fructotransferase.,Park J, Kim MI, Park YD, Shin I, Cha J, Kim CH, Rhee S J Biol Chem. 2012 Jul 18. PMID:22810228<ref>PMID:22810228</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arthrobacter ureafaciens]]
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[[Category: Large Structures]]
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[[Category: Park, J.]]
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[[Category: Paenarthrobacter ureafaciens]]
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[[Category: Rhee, S.]]
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[[Category: Park J]]
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[[Category: Glycoside hydrolase]]
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[[Category: Rhee S]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of Levan Fructotransferase D54N mutant from Arthrobacter ureafaciens in complex with levanbiose

PDB ID 4ffi

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