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The structure of LL-diaminopimelate aminotransferase from Chlamydia trachomatis: implications for its broad substrate specificity.

Abstract：

:We have previously reported the structures of the native holo and substrate-bound forms of LL-diaminopimelate aminotransferase from Arabidopsis thaliana (AtDAP-AT). Here, we report the crystal and molecular structures of the LL-diaminopimelate aminotransferase from Chlamydia trachomatis (CtDAP-AT) in the apo-form and the pyridoxal-5'-phosphate-bound form. The molecular structure of CtDAP-AT shows that its overall fold is essentially identical with that of AtDAP-AT except that CtDAP-AT adopts an "open" conformation as opposed to the "closed" conformation of AtDAP-AT. Although AtDAP-AT and CtDAP-AT are approximately 40% identical in their primary sequence, they have major differences in their substrate specificities; AtDAP-AT is highly specific for LL-DAP, whereas CtDAP-AT accepts a wider range of substrates. Since all of the residues involved in substrate recognition are highly conserved between AtDAP-AT and CtDAP-AT, we propose that differences in flexibility of the loops lining the active-site region between the two enzymes likely account for the differences in substrate specificity.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Watanabe N,Clay MD,van Belkum MJ,Fan C,Vederas JC,James MN

doi

10.1016/j.jmb.2011.06.023

subject

Has Abstract

pub_date

2011-08-19 00:00:00

pages

649-60

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(11)00669-3

journal_volume

411

pub_type

杂志文章

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