4itb: Difference between revisions

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-'''Unreleased structure'''
-The entry 4itb is ON HOLD
+==Structure of bacterial enzyme in complex with cofactor and substrate==
+<StructureSection load='4itb' size='340' side='right'caption='[[4itb]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4itb]] 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=4ITB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ITB FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</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=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=SSN:4-OXOBUTANOIC+ACID'>SSN</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=4itb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4itb OCA], [https://pdbe.org/4itb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4itb RCSB], [https://www.ebi.ac.uk/pdbsum/4itb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4itb ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-Authors: Rhee, S., Park, J.
+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>
-Description: Structure of bacterial enzyme in complex with cofactor and substrate
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4itb" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Succinate-semialdehyde dehydrogenase|Succinate-semialdehyde dehydrogenase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Synechococcus sp. PCC 7002]]
+[[Category: Park J]]
+[[Category: Rhee S]]