1l5j
From Proteopedia
(New page: 200px<br /><applet load="1l5j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l5j, resolution 2.40Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1l5j.gif|left|200px]]<br /><applet load="1l5j" size=" | + | [[Image:1l5j.gif|left|200px]]<br /><applet load="1l5j" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1l5j, resolution 2.40Å" /> | caption="1l5j, resolution 2.40Å" /> | ||
'''CRYSTAL STRUCTURE OF E. COLI ACONITASE B.'''<br /> | '''CRYSTAL STRUCTURE OF E. COLI ACONITASE B.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The major bifunctional aconitase of Escherichia coli (AcnB) serves as | + | 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== | ==About this Structure== | ||
| - | 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 TRA and F3S 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Artymiuk, P | + | [[Category: Artymiuk, P J.]] |
| - | [[Category: Barynin, V | + | [[Category: Barynin, V V.]] |
[[Category: Green, J.]] | [[Category: Green, J.]] | ||
| - | [[Category: Guest, J | + | [[Category: Guest, J R.]] |
| - | [[Category: Sedelnikova, S | + | [[Category: Sedelnikova, S E.]] |
| - | [[Category: Stillman, T | + | [[Category: Stillman, T J.]] |
[[Category: Tang, Y.]] | [[Category: Tang, Y.]] | ||
| - | [[Category: Williams, C | + | [[Category: Williams, C H.]] |
[[Category: F3S]] | [[Category: F3S]] | ||
[[Category: TRA]] | [[Category: TRA]] | ||
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[[Category: rna binding]] | [[Category: rna binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:41:39 2008'' |
Revision as of 11:41, 21 February 2008
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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 with and as ligands. Active as Aconitate hydratase, with EC number 4.2.1.3 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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