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| | ==Crystal structure of KGPDC from Streptococcus mutans== | | ==Crystal structure of KGPDC from Streptococcus mutans== |
| - | <StructureSection load='3exr' size='340' side='right' caption='[[3exr]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='3exr' size='340' side='right'caption='[[3exr]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3exr]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25175 Atcc 25175]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EXR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3exr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EXR FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3exs|3exs]], [[3ext|3ext]]</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]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ulaD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1309 ATCC 25175])</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=3exr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exr OCA], [https://pdbe.org/3exr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3exr RCSB], [https://www.ebi.ac.uk/pdbsum/3exr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3exr 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/3-dehydro-L-gulonate-6-phosphate_decarboxylase 3-dehydro-L-gulonate-6-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.85 4.1.1.85] </span></td></tr>
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| - | <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=3exr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3exr OCA], [http://pdbe.org/3exr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3exr RCSB], [http://www.ebi.ac.uk/pdbsum/3exr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3exr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q93DA8_STRMG Q93DA8_STRMG] |
| | == 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: 3-dehydro-L-gulonate-6-phosphate decarboxylase]] | + | [[Category: Large Structures]] |
| - | [[Category: Atcc 25175]] | + | [[Category: Streptococcus mutans]] |
| - | [[Category: Li, G L]] | + | [[Category: Li GL]] |
| - | [[Category: Li, L F]] | + | [[Category: Li LF]] |
| - | [[Category: Liu, X]] | + | [[Category: Liu X]] |
| - | [[Category: Su, X D]] | + | [[Category: Su XD]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Lyase]]
| + | |
| Structural highlights
Function
Q93DA8_STRMG
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
The 3-keto-L-gulonate 6-phosphate decarboxylase (KGPDC) catalyses the decarboxylation of 3-keto-L-gulonate 6-phosphate to L-xylulose in the presence of magnesium ions. The enzyme is involved in L-ascorbate metabolism and plays an essential role in the pathway of glucuronate interconversion. Crystal structures of Streptococcus mutans KGPDC were determined in the absence and presence of the product analog D-ribulose 5-phosphate. We have observed an 8 A alphaB-helix movement and other structural rearrangements around the active site between the apo-structures and product analog bound structure. These drastic conformational changes upon ligand binding are the first observation of this kind for the KGPDC family. The flexibilities of both the alpha-helix lid and the side chains of Arg144 and Arg197 are associated with substrate binding and product releasing. The open-closed conformational changes of the active site, through the movements of the alpha-helix lid and the arginine residues are important for substrate binding and catalysis.
Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans.,Li GL, Liu X, Nan J, Brostromer E, Li LF, Su XD Biochem Biophys Res Commun. 2009 Apr 10;381(3):429-33. Epub 2009 Feb 15. PMID:19222992[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li GL, Liu X, Nan J, Brostromer E, Li LF, Su XD. Open-closed conformational change revealed by the crystal structures of 3-keto-L-gulonate 6-phosphate decarboxylase from Streptococcus mutans. Biochem Biophys Res Commun. 2009 Apr 10;381(3):429-33. Epub 2009 Feb 15. PMID:19222992 doi:10.1016/j.bbrc.2009.02.049
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