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| ==Structure of Bacterial Enzyme== | | ==Structure of Bacterial Enzyme== |
| <StructureSection load='4it9' size='340' side='right' caption='[[4it9]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4it9' size='340' side='right'caption='[[4it9]], [[Resolution|resolution]] 1.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[4it9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Agmenellum_quadruplicatum Agmenellum quadruplicatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IT9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IT9 FirstGlance]. <br> | | <table><tr><td colspan='2'>[[4it9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._PCC_7002 Synechococcus sp. PCC 7002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IT9 FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 1.7Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ita|4ita]], [[4itb|4itb]]</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4it9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4it9 OCA], [http://pdbe.org/4it9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4it9 RCSB], [http://www.ebi.ac.uk/pdbsum/4it9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4it9 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=4it9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4it9 OCA], [https://pdbe.org/4it9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4it9 RCSB], [https://www.ebi.ac.uk/pdbsum/4it9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4it9 ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/B1XMM6_SYNP2 B1XMM6_SYNP2] |
| Succinic semialdehyde dehydrogenase (SSADH) from cyanobacterium Synechococcus differs from other SSADHs in the gamma-aminobutyrate shunt. Synechococcus SSADH (SySSADH) is a TCA cycle enzyme and completes a 2-oxoglutarate dehydrogenase-deficient cyanobacterial TCA cycle through a detour metabolic pathway. SySSADH produces succinate in an NADP(+)-dependent manner with a single cysteine acting as the catalytic residue in the catalytic loop. Crystal structures of SySSADH were determined in their apo form, as a binary complex with NADP(+) and as a ternary complex with succinic semialdehyde and NADPH, providing details about the catalytic mechanism by revealing a covalent adduct of a cofactor with the catalytic cysteine in the binary complex and a proposed thiohemiacetal intermediate in the ternary complex. Further analyses showed that SySSADH is an oxidation-sensitive enzyme and that the formation of the NADP-cysteine adduct is a kinetically preferred event that protects the catalytic cysteine from H2O2-dependent oxidative stress. These structural and functional features of SySSADH provide a molecular basis for cofactor-dependent oxidation protection in 1-Cys SSADH, which is unique relative to other 2-Cys SSADHs employing a redox-dependent formation of a disulfide bridge.
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| Structural Basis for a Cofactor-dependent Oxidation Protection and Catalysis of Cyanobacterial Succinic Semialdehyde Dehydrogenase.,Park J, Rhee S J Biol Chem. 2013 May 31;288(22):15760-70. doi: 10.1074/jbc.M113.460428. Epub, 2013 Apr 15. PMID:23589281<ref>PMID:23589281</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 4it9" style="background-color:#fffaf0;"></div>
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| ==See Also== | | ==See Also== |
| *[[Succinate-semialdehyde dehydrogenase|Succinate-semialdehyde dehydrogenase]] | | *[[Succinate-semialdehyde dehydrogenase|Succinate-semialdehyde dehydrogenase]] |
| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Agmenellum quadruplicatum]] | | [[Category: Large Structures]] |
| [[Category: Park, J]] | | [[Category: Synechococcus sp. PCC 7002]] |
| [[Category: Rhee, S]] | | [[Category: Park J]] |
| [[Category: Oxidoreductase]] | | [[Category: Rhee S]] |
| [[Category: Rossmann fold]]
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