|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3gtd' size='340' side='right'caption='[[3gtd]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='3gtd' size='340' side='right'caption='[[3gtd]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3gtd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ricpr Ricpr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GTD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gtd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rickettsia_prowazekii_str._Madrid_E Rickettsia prowazekii str. Madrid E]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GTD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GTD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2.4Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fumC, RP665 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272947 RICPR])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Fumarate_hydratase Fumarate hydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2] </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=3gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gtd OCA], [https://pdbe.org/3gtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gtd RCSB], [https://www.ebi.ac.uk/pdbsum/3gtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gtd 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=3gtd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gtd OCA], [https://pdbe.org/3gtd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gtd RCSB], [https://www.ebi.ac.uk/pdbsum/3gtd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gtd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/FUMC_RICPR FUMC_RICPR]] Catalyzes the reversible addition of water to fumarate to give L-malate (By similarity).[HAMAP-Rule:MF_00743]
| + | [https://www.uniprot.org/uniprot/FUMC_RICPR FUMC_RICPR] Catalyzes the reversible addition of water to fumarate to give L-malate (By similarity).[HAMAP-Rule:MF_00743] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 37: |
Line 36: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Fumarate hydratase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ricpr]] | + | [[Category: Rickettsia prowazekii str. Madrid E]] |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Fumarate]]
| + | |
| - | [[Category: Hydratase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Ssgcid]]
| + | |
| - | [[Category: Tricarboxylic acid cycle]]
| + | |
| Structural highlights
Function
FUMC_RICPR Catalyzes the reversible addition of water to fumarate to give L-malate (By similarity).[HAMAP-Rule:MF_00743]
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
Rickettsiae are obligate intracellular parasites of eukaryotic cells that are the causative agents responsible for spotted fever and typhus. Their small genome (about 800 protein-coding genes) is highly conserved across species and has been postulated as the ancestor of the mitochondria. No genes that are required for glycolysis are found in the Rickettsia prowazekii or mitochondrial genomes, but a complete set of genes encoding components of the tricarboxylic acid cycle and the respiratory-chain complex is found in both. A 2.4 A resolution crystal structure of R. prowazekii fumarate hydratase, an enzyme catalyzing the third step of the tricarboxylic acid cycle pathway that ultimately converts phosphoenolpyruvate into succinyl-CoA, has been solved. A structure alignment with human mitochondrial fumarate hydratase highlights the close similarity between R. prowazekii and mitochondrial enzymes.
Structure of fumarate hydratase from Rickettsia prowazekii, the agent of typhus and suspected relative of the mitochondria.,Phan I, Subramanian S, Olsen C, Edwards TE, Guo W, Zhang Y, Van Voorhis WC, Stewart LJ, Myler PJ Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1123-8. Epub 2011 Aug 16. PMID:21904061[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Phan I, Subramanian S, Olsen C, Edwards TE, Guo W, Zhang Y, Van Voorhis WC, Stewart LJ, Myler PJ. Structure of fumarate hydratase from Rickettsia prowazekii, the agent of typhus and suspected relative of the mitochondria. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1123-8. Epub 2011 Aug 16. PMID:21904061 doi:10.1107/S174430911102690X
|
