1l5j: Difference between revisions

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<StructureSection load='1l5j' size='340' side='right'caption='[[1l5j]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1l5j' size='340' side='right'caption='[[1l5j]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1l5j]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. 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>
<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='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>
</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>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aconitate_hydratase Aconitate hydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.3 4.2.1.3] </span></td></tr>
<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'>[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>
<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/ACON2_ECOLI ACON2_ECOLI]] Catalyzes the isomerization of citrate to isocitrate via cis-aconitate as well as the dehydration of 2-methylisocitrate to cis-2-methylaconitate.  
[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.
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:11992126<ref>PMID:11992126</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1l5j" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Aconitate hydratase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Artymiuk, P J]]
[[Category: Artymiuk PJ]]
[[Category: Barynin, V V]]
[[Category: Barynin VV]]
[[Category: Green, J]]
[[Category: Green J]]
[[Category: Guest, J R]]
[[Category: Guest JR]]
[[Category: Sedelnikova, S E]]
[[Category: Sedelnikova SE]]
[[Category: Stillman, T J]]
[[Category: Stillman TJ]]
[[Category: Tang, Y]]
[[Category: Tang Y]]
[[Category: Williams, C H]]
[[Category: Williams CH]]
[[Category: Citric acid cycle]]
[[Category: Heat-like domain]]
[[Category: Lyase]]
[[Category: Molecular recognition]]
[[Category: Rna binding]]

Revision as of 07:29, 14 February 2024

CRYSTAL STRUCTURE OF E. COLI ACONITASE B.

1l5j, resolution 2.40Å

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