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2qb2

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{{STRUCTURE_2qb2| PDB=2qb2 | SCENE= }}
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'''Structural Studies Reveal the Inactivation of E. coli L-aspartate aminotransferase by (s)-4,5-dihydro-2thiophenecarboylic acid (SADTA) via two mechanisms (at pH 7.0).'''
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===Structural Studies Reveal the Inactivation of E. coli L-aspartate aminotransferase by (s)-4,5-dihydro-2thiophenecarboylic acid (SADTA) via two mechanisms (at pH 7.0).===
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==Overview==
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As a mechanism-based inactivator of PLP-enzymes, (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid (SADTA) was cocrystallized with Escherichia coli aspartate aminotransferase (l-AspAT) at a series of pH values ranging from 6 to 8. Five structural models with high resolution (1.4-1.85 A) were obtained for l-AspAT-SADTA complexes at pH 6.0, 6.5, 7.0, 7.5, and 8.0. Electron densities of the models showed that two different adducts had formed in the active sites. One adduct was formed from SADTA covalently linked to pyridoxal 5'-phosphate (PLP) while the other adduct was formed with the inhibitor covalently linked to Lysine246,1 the active site lysine. Moreover, there is a strong indication based on the electron densities that the occurrence of the two adducts is pH dependent. We conclude that SADTA inactivates l-AspAT via two different mechanisms based on the binding direction of the inactivator. Additionally, the structural models also show pH dependence of the protein structure itself, which provided detailed mechanistic implications for l-AspAT.
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(as it appears on PubMed at http://www.pubmed.gov), where 17713924 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17713924}}
==About this Structure==
==About this Structure==
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[[Category: Plp]]
[[Category: Plp]]
[[Category: Sadta]]
[[Category: Sadta]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:39:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:32:08 2008''

Revision as of 17:32, 28 July 2008

Image:2qb2.png

Template:STRUCTURE 2qb2

Structural Studies Reveal the Inactivation of E. coli L-aspartate aminotransferase by (s)-4,5-dihydro-2thiophenecarboylic acid (SADTA) via two mechanisms (at pH 7.0).

Template:ABSTRACT PUBMED 17713924

About this Structure

2QB2 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals "a tale of two mechanisms"., Liu D, Pozharski E, Lepore BW, Fu M, Silverman RB, Petsko GA, Ringe D, Biochemistry. 2007 Sep 18;46(37):10517-27. Epub 2007 Aug 22. PMID:17713924

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