1l5j
From Proteopedia
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==CRYSTAL STRUCTURE OF E. COLI ACONITASE B.== | ==CRYSTAL STRUCTURE OF E. COLI ACONITASE B.== | ||
| - | <StructureSection load='1l5j' size='340' side='right' caption='[[1l5j]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='1l5j' size='340' side='right'caption='[[1l5j]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1l5j]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1l5j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L5J FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </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=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=TRA:ACONITATE+ION'>TRA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5j OCA], [https://pdbe.org/1l5j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l5j RCSB], [https://www.ebi.ac.uk/pdbsum/1l5j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l5j ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/ACNB_ECOLI ACNB_ECOLI] Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein. During oxidative stress inactive AcnB apo-enzyme without iron sulfur clusters binds the acnB mRNA 3' UTRs (untranslated regions), stabilizes acnB mRNA and increases AcnB synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnB also decreases the stability of the sodA transcript.<ref>PMID:10585860</ref> <ref>PMID:10589714</ref> <ref>PMID:11932448</ref> <ref>PMID:12473114</ref> <ref>PMID:15882410</ref> <ref>PMID:8000525</ref> <ref>PMID:8932712</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l5j ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1l5j ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The major bifunctional aconitase of Escherichia coli (AcnB) serves as either an enzymic catalyst or a mRNA-binding post-transcriptional regulator, depending on the status of its iron sulfur cluster. AcnB represents a large, distinct group of Gram-negative bacterial aconitases that have an altered domain organization relative to mitochondrial aconitase and other aconitases. Here the 2.4 A structure of E. coli AcnB reveals a high degree of conservation at the active site despite its domain reorganization. It also reveals that the additional domain, characteristic of the AcnB subfamily, is a HEAT-like domain, implying a role in protein protein recognition. This domain packs against the remainder of the protein to form a tunnel leading to the aconitase active site, potentially for substrate channeling. | ||
| - | + | ==See Also== | |
| - | + | *[[Aconitase 3D structures|Aconitase 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Artymiuk | + | [[Category: Artymiuk PJ]] |
| - | [[Category: Barynin | + | [[Category: Barynin VV]] |
| - | [[Category: Green | + | [[Category: Green J]] |
| - | [[Category: Guest | + | [[Category: Guest JR]] |
| - | [[Category: Sedelnikova | + | [[Category: Sedelnikova SE]] |
| - | [[Category: Stillman | + | [[Category: Stillman TJ]] |
| - | [[Category: Tang | + | [[Category: Tang Y]] |
| - | [[Category: Williams | + | [[Category: Williams CH]] |
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Current revision
CRYSTAL STRUCTURE OF E. COLI ACONITASE B.
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