2a4n

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(New page: 200px<br /><applet load="2a4n" size="350" color="white" frame="true" align="right" spinBox="true" caption="2a4n, resolution 2.200&Aring;" /> '''Crystal structure o...)
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==Overview==
==Overview==
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The aminoglycoside-modifying enzyme aminoglycoside 6'-N-acetyltransferase, type Ii [AAC(6')-Ii] has been crystallized with its cofactor coenzyme A in, space group C222(1), with unit-cell parameters a = 71.5, b = 127.4, c =, 76.9 A and one physiologically relevant dimer species per asymmetric unit., The space group previously observed for this complex was P2(1)2(1)2(1), with two dimers per asymmetric unit. By comparing the six available, protomer structures of the AAC(6')-Ii-CoA complex, it has been possible to, identify regions of plasticity within the protein. Normal-mode analysis of, this complex suggests that this plasticity is not an artefact of, crystal-packing forces, but that the region of the protomer that displays, multiple conformations is intrinsically flexible. It is conjectured that, the flexibility is relevant for the cooperative activity observed for the, enzyme.
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The aminoglycoside-modifying enzyme aminoglycoside 6'-N-acetyltransferase type Ii [AAC(6')-Ii] has been crystallized with its cofactor coenzyme A in space group C222(1), with unit-cell parameters a = 71.5, b = 127.4, c = 76.9 A and one physiologically relevant dimer species per asymmetric unit. The space group previously observed for this complex was P2(1)2(1)2(1), with two dimers per asymmetric unit. By comparing the six available protomer structures of the AAC(6')-Ii-CoA complex, it has been possible to identify regions of plasticity within the protein. Normal-mode analysis of this complex suggests that this plasticity is not an artefact of crystal-packing forces, but that the region of the protomer that displays multiple conformations is intrinsically flexible. It is conjectured that the flexibility is relevant for the cooperative activity observed for the enzyme.
==About this Structure==
==About this Structure==
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[[Category: Enterococcus faecium]]
[[Category: Enterococcus faecium]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Berghuis, A.M.]]
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[[Category: Berghuis, A M.]]
[[Category: Breitbach, C.]]
[[Category: Breitbach, C.]]
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[[Category: Burk, D.L.]]
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[[Category: Burk, D L.]]
[[Category: Xiong, B.]]
[[Category: Xiong, B.]]
[[Category: COA]]
[[Category: COA]]
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[[Category: n-acetyl transferase]]
[[Category: n-acetyl transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:54:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:23:36 2008''

Revision as of 14:23, 21 February 2008


2a4n, resolution 2.200Å

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Crystal structure of aminoglycoside 6'-N-acetyltransferase complexed with coenzyme A

Overview

The aminoglycoside-modifying enzyme aminoglycoside 6'-N-acetyltransferase type Ii [AAC(6')-Ii] has been crystallized with its cofactor coenzyme A in space group C222(1), with unit-cell parameters a = 71.5, b = 127.4, c = 76.9 A and one physiologically relevant dimer species per asymmetric unit. The space group previously observed for this complex was P2(1)2(1)2(1), with two dimers per asymmetric unit. By comparing the six available protomer structures of the AAC(6')-Ii-CoA complex, it has been possible to identify regions of plasticity within the protein. Normal-mode analysis of this complex suggests that this plasticity is not an artefact of crystal-packing forces, but that the region of the protomer that displays multiple conformations is intrinsically flexible. It is conjectured that the flexibility is relevant for the cooperative activity observed for the enzyme.

About this Structure

2A4N is a Single protein structure of sequence from Enterococcus faecium with and as ligands. Active as Aminoglycoside N(6')-acetyltransferase, with EC number 2.3.1.82 Full crystallographic information is available from OCA.

Reference

Structures of aminoglycoside acetyltransferase AAC(6')-Ii in a novel crystal form: structural and normal-mode analyses., Burk DL, Xiong B, Breitbach C, Berghuis AM, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1273-9. Epub 2005, Aug 16. PMID:16131761

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