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1l5j

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[[Image:1l5j.gif|left|200px]]<br /><applet load="1l5j" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1l5j, resolution 2.40&Aring;" />
 
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'''CRYSTAL STRUCTURE OF E. COLI ACONITASE B.'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF E. COLI ACONITASE B.==
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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.
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<StructureSection load='1l5j' size='340' side='right'caption='[[1l5j]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<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>
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<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>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l5/1l5j_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1L5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=TRA:'>TRA</scene> and <scene name='pdbligand=F3S:'>F3S</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aconitate_hydratase Aconitate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.3 4.2.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L5J OCA].
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*[[Aconitase 3D structures|Aconitase 3D structures]]
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== References ==
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==Reference==
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<references/>
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E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition., Williams CH, Stillman TJ, Barynin VV, Sedelnikova SE, Tang Y, Green J, Guest JR, Artymiuk PJ, Nat Struct Biol. 2002 Jun;9(6):447-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11992126 11992126]
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__TOC__
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[[Category: Aconitate hydratase]]
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Artymiuk, P J.]]
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[[Category: Artymiuk PJ]]
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[[Category: Barynin, V V.]]
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[[Category: Barynin VV]]
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[[Category: Green, J.]]
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[[Category: Green J]]
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[[Category: Guest, J R.]]
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[[Category: Guest JR]]
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[[Category: Sedelnikova, S E.]]
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[[Category: Sedelnikova SE]]
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[[Category: Stillman, T J.]]
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[[Category: Stillman TJ]]
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[[Category: Tang, Y.]]
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[[Category: Tang Y]]
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[[Category: Williams, C H.]]
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[[Category: Williams CH]]
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[[Category: F3S]]
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[[Category: TRA]]
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[[Category: citric acid cycle]]
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[[Category: heat-like domain]]
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[[Category: molecular recognition]]
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[[Category: rna binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:39 2008''
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Current revision

CRYSTAL STRUCTURE OF E. COLI ACONITASE B.

PDB ID 1l5j

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