1l5j

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[[Image:1l5j.gif|left|200px]]
[[Image:1l5j.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1l5j |SIZE=350|CAPTION= <scene name='initialview01'>1l5j</scene>, resolution 2.40&Aring;
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The line below this paragraph, containing "STRUCTURE_1l5j", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=TRA:ACONITATE+ION'>TRA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1l5j| PDB=1l5j | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l5j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l5j OCA], [http://www.ebi.ac.uk/pdbsum/1l5j PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1l5j RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF E. COLI ACONITASE B.'''
'''CRYSTAL STRUCTURE OF E. COLI ACONITASE B.'''
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[[Category: Tang, Y.]]
[[Category: Tang, Y.]]
[[Category: Williams, C H.]]
[[Category: Williams, C H.]]
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[[Category: citric acid cycle]]
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[[Category: Citric acid cycle]]
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[[Category: heat-like domain]]
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[[Category: Heat-like domain]]
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[[Category: molecular recognition]]
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[[Category: Molecular recognition]]
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[[Category: rna binding]]
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[[Category: Rna binding]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:33:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:58:21 2008''
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Revision as of 20:33, 2 May 2008

Template:STRUCTURE 1l5j

CRYSTAL STRUCTURE OF E. COLI ACONITASE B.


Overview

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.

About this Structure

1L5J is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 23:33:52 2008

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