3ASA

Crystal structure of apo-LL-diaminopimelate aminotransferase from Chlamydia trachomatis

Summary for 3ASA

• Entry DOI: 10.2210/pdb3asa/pdb
• Related: 3ASB
• Descriptor: LL-diaminopimelate aminotransferase (2 entities in total)
• Functional Keywords: plp dependent aminotransferase, transferase
• Biological source: Chlamydia trachomatis
• Total number of polymer chains: 1
• Total formula weight: 44712.64

Authors

Watanabe, N.,James, M.N. (deposition date: 2010-12-10, release date: 2011-08-31, Last modification date: 2024-03-13)

Primary citation

Watanabe, N.,Clay, M.D.,van Belkum, M.J.,Fan, C.,Vederas, J.C.,James, M.N.
The Structure of ll-Diaminopimelate Aminotransferase from Chlamydia trachomatis: Implications for Its Broad Substrate Specificity.
J.Mol.Biol., 411:649-660, 2011

PubMed 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.

PubMed: 21722650
DOI: 10.1016/j.jmb.2011.06.023

Experimental method

X-RAY DIFFRACTION (2.05 Å)