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2z20

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[[Image:2z20.gif|left|200px]]
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{{STRUCTURE_2z20| PDB=2z20 | SCENE= }}
{{STRUCTURE_2z20| PDB=2z20 | SCENE= }}
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'''Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana'''
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===Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana===
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==Overview==
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The essential biosynthetic pathway to l-Lysine in bacteria and plants is an attractive target for the development of new antibiotics or herbicides because it is absent in humans, who must acquire this amino acid in their diet. Plants use a shortcut of a bacterial pathway to l-Lysine in which the pyridoxal-5'-phosphate (PLP)-dependent enzyme ll-diaminopimelate aminotransferase (LL-DAP-AT) transforms l-tetrahydrodipicolinic acid (L-THDP) directly to LL-DAP. In addition, LL-DAP-AT was recently found in Chlamydia sp., suggesting that inhibitors of this enzyme may also be effective against such organisms. In order to understand the mechanism of this enzyme and to assist in the design of inhibitors, the three-dimensional crystal structure of LL-DAP-AT was determined at 1.95 A resolution. The cDNA sequence of LL-DAP-AT from Arabidopsis thaliana (AtDAP-AT) was optimized for expression in bacteria and cloned in Escherichia coli without its leader sequence but with a C-terminal hexahistidine affinity tag to aid protein purification. The structure of AtDAP-AT was determined using the multiple-wavelength anomalous dispersion (MAD) method with a seleno-methionine derivative. AtDAP-AT is active as a homodimer with each subunit having PLP in the active site. It belongs to the family of type I fold PLP-dependent enzymes. Comparison of the active site residues of AtDAP-AT and aspartate aminotransferases revealed that the PLP binding residues in AtDAP-AT are well conserved in both enzymes. However, Glu97* and Asn309* in the active site of AtDAP-AT are not found at similar positions in aspartate aminotransferases, suggesting that specific substrate recognition may require these residues from the other monomer. A malate-bound structure of AtDAP-AT allowed LL-DAP and L-glutamate to be modelled into the active site. These initial three-dimensional structures of LL-DAP-AT provide insight into its substrate specificity and catalytic mechanism.
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(as it appears on PubMed at http://www.pubmed.gov), where 17583737 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17583737}}
==About this Structure==
==About this Structure==
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[[Category: Plp]]
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[[Category: Thdpa]]
[[Category: Thdpa]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 19:50:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:21:37 2008''

Revision as of 08:21, 28 July 2008

Image:2z20.png

Template:STRUCTURE 2z20

Crystal structure of LL-Diaminopimelate Aminotransferase from Arabidopsis thaliana

Template:ABSTRACT PUBMED 17583737

About this Structure

2Z20 is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis thaliana: a recently discovered enzyme in the biosynthesis of L-lysine by plants and Chlamydia., Watanabe N, Cherney MM, van Belkum MJ, Marcus SL, Flegel MD, Clay MD, Deyholos MK, Vederas JC, James MN, J Mol Biol. 2007 Aug 17;371(3):685-702. Epub 2007 May 26. PMID:17583737

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