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1l5j
From Proteopedia
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| - | [[Image:1l5j.gif|left|200px]] | + | [[Image:1l5j.gif|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF E. COLI ACONITASE B.''' | + | {{Structure |
| + | |PDB= 1l5j |SIZE=350|CAPTION= <scene name='initialview01'>1l5j</scene>, resolution 2.40Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=TRA:ACONITATE+ION'>TRA</scene> and <scene name='pdbligand=F3S:FE3-S4 CLUSTER'>F3S</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF E. COLI ACONITASE B.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L5J is a [ | + | 1L5J is a [[Single protein]] structure of sequence from [http://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]. |
==Reference== | ==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:[http:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/11992126 11992126] |
[[Category: Aconitate hydratase]] | [[Category: Aconitate hydratase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: rna binding]] | [[Category: rna binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:26:40 2008'' |
Revision as of 10:26, 20 March 2008
| |||||||
| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Aconitate hydratase, with EC number 4.2.1.3 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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