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| | <StructureSection load='1c4k' size='340' side='right'caption='[[1c4k]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='1c4k' size='340' side='right'caption='[[1c4k]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1c4k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lacs3 Lacs3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C4K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1c4k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactobacillus_sp._30A Lactobacillus sp. 30A]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C4K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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]] 2.7Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ornithine_decarboxylase Ornithine decarboxylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.17 4.1.1.17] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></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=1c4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4k OCA], [https://pdbe.org/1c4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c4k RCSB], [https://www.ebi.ac.uk/pdbsum/1c4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4k ProSAT]</span></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=1c4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c4k OCA], [https://pdbe.org/1c4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c4k RCSB], [https://www.ebi.ac.uk/pdbsum/1c4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c4k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/DCOR_LACS3 DCOR_LACS3] |
| | == 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: Lacs3]] | + | [[Category: Lactobacillus sp. 30A]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ornithine decarboxylase]]
| + | [[Category: Hackert ML]] |
| - | [[Category: Hackert, M L]] | + | [[Category: Vitali J]] |
| - | [[Category: Vitali, J]] | + | |
| - | [[Category: Decarboxylase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Ornithine]]
| + | |
| Structural highlights
Function
DCOR_LACS3
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
Ornithine decarboxylases catalyze the conversion of ornithine to putrescine at the beginning of the polyamine pathway. Ornithine decarboxylase (ODC) from Lactobacillus 30a is a 990612 Da dodecamer composed of six homodimers. A single point mutation (Gly121Tyr) was found to prevent association of dimers into dodecamers. The dimeric protein has been crystallized at pH 7.0 in the presence of guanosine triphosphate (GTP). Crystals belong to space group P3(2)21, with unit-cell parameters a = 111.8, c = 135.9 A and one monomer in the asymmetric unit. The structure was determined by molecular replacement and refined using simulated annealing to R = 0.211 at 2. 7 A resolution. The GTP-binding site was analyzed in detail. The protein exhibits a novel binding mode for GTP which is different from that seen in most G-proteins or GTPases. Central to this binding scheme appear to be three lysines, Lys190, Lys374 and Lys382, which form salt bridges with the three phosphates, and Thr191, which hydrogen bonds with the guanine base. Furthermore, the structure suggests that there is some flexibility in the wing domain, which can change its orientation as the protein adapts to its environment. The active site is similar to that of the native enzyme, consistent with the observation that the enzyme activity does not depend on its dodecameric state.
Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a.,Vitali J, Carroll D, Chaudhry RG, Hackert ML Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):1978-85. PMID:10666573[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vitali J, Carroll D, Chaudhry RG, Hackert ML. Three-dimensional structure of the Gly121Tyr dimeric form of ornithine decarboxylase from Lactobacillus 30a. Acta Crystallogr D Biol Crystallogr. 1999 Dec;55(Pt 12):1978-85. PMID:10666573
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