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| | <StructureSection load='1m53' size='340' side='right'caption='[[1m53]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='1m53' size='340' side='right'caption='[[1m53]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1m53]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Klebsiella_sp._lx3 Klebsiella sp. lx3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M53 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1M53 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1m53]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_sp._LX3 Klebsiella sp. LX3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M53 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1uok|1uok]], [[1g5a|1g5a]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PalI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=167956 Klebsiella sp. LX3])</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=1m53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m53 OCA], [https://pdbe.org/1m53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m53 RCSB], [https://www.ebi.ac.uk/pdbsum/1m53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m53 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isomaltulose_synthase Isomaltulose synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.11 5.4.99.11] </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=1m53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m53 OCA], [http://pdbe.org/1m53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m53 RCSB], [http://www.ebi.ac.uk/pdbsum/1m53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m53 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8KR84_9ENTR Q8KR84_9ENTR] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Isomaltulose synthase]]
| + | [[Category: Klebsiella sp. LX3]] |
| - | [[Category: Klebsiella sp. lx3]] | + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, N]] | + | [[Category: Li N]] |
| - | [[Category: Swaminathan, K]] | + | [[Category: Swaminathan K]] |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Sucrose isomerization]]
| + | |
| Structural highlights
Function
Q8KR84_9ENTR
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Isomaltulose synthase from Klebsiella sp. LX3 (PalI, EC 5.4.99.11) catalyzes the isomerization of sucrose to produce isomaltulose (alpha-D-glucosylpyranosyl-1,6-D-fructofuranose) and trehalulose (alpha-D-glucosylpyranosyl-1,1-d-fructofuranose). The PalI structure, solved at 2.2-A resolution with an R-factor of 19.4% and Rfree of 24.2%, consists of three domains: an N-terminal catalytic (beta/alpha)8 domain, a subdomain between N beta 3 and N alpha 3, and a C-terminal domain having seven beta-strands. The active site architecture of PalI is identical to that of other glycoside hydrolase family 13 members, suggesting a similar mechanism in substrate binding and hydrolysis. However, a unique RLDRD motif in the proximity of the active site has been identified and shown biochemically to be responsible for sucrose isomerization. A two-step reaction mechanism for hydrolysis and isomerization, which occurs in the same pocket is proposed based on both the structural and biochemical data. Selected C-terminal truncations have been shown to reduce and even abolish the enzyme activity, consistent with the predicted role of the C-terminal residues in the maintenance of enzyme conformation and active site topology.
Isomaltulose synthase (PalI) of Klebsiella sp. LX3. Crystal structure and implication of mechanism.,Zhang D, Li N, Lok SM, Zhang LH, Swaminathan K J Biol Chem. 2003 Sep 12;278(37):35428-34. Epub 2003 Jun 20. PMID:12819210[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zhang D, Li N, Lok SM, Zhang LH, Swaminathan K. Isomaltulose synthase (PalI) of Klebsiella sp. LX3. Crystal structure and implication of mechanism. J Biol Chem. 2003 Sep 12;278(37):35428-34. Epub 2003 Jun 20. PMID:12819210 doi:http://dx.doi.org/10.1074/jbc.M302616200
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