Structural highlights
3ht5 is a 1 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | |
| Related: | 2hhf, 1kt8, 1iyd |
| Gene: | ilvE, MT2266, MTCY190.21c, Rv2210c ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) |
| Activity: | Branched-chain-amino-acid transaminase, with EC number 2.6.1.42 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[ILVE_MYCTU] Catalyzes the reversible transfers of an amino group from glutamate to the alpha-ketoacid of the respective amino acid in the final step in the biosynthesis of branchedchain amino acids. The amino acids can be ranked in the following order with respect to their efficiency as amino donor: Leu > Ile > Val.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Unlike mammals, bacteria encode enzymes that synthesize branched-chain amino acids. The pyridoxal 50-phosphate-dependent transaminase performs the final biosynthetic step in these pathways, converting keto acid precursors into -amino acids. The branched-chain amino-acid transaminase from Mycobacterium tuberculosis (MtIlvE) has been crystallized and its structure has been solved at 1.9 angstrom resolution. The MtIlvE monomer is composed of two domains that interact to form the active site. The biologically active form of IlvE is a homodimer in which each monomer contributes a substrate-specificity loop to the partner molecule. Additional substrate selectivity may be imparted by a conserved N-terminal Phe30 residue, which has previously been observed to shield the active site in the type IV fold homodimer. The active site of MtIlvE contains density corresponding to bound PMP, which is likely to be a consequence of the presence of tryptone in the crystallization medium. Additionally, two cysteine residues are positioned at the dimer interface for disulfide-bond formation under oxidative conditions. It is unknown whether they are involved in any regulatory activities analogous to those of the human mitochondrial branched-chain amino-acid transaminase.
The 1.9 A structure of the branched-chain amino-acid transaminase (IlvE) from Mycobacterium tuberculosis.,Tremblay LW, Blanchard JS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt, 11):1071-7. Epub 2009 Oct 13. PMID:19923721[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Castell A, Mille C, Unge T. Structural analysis of mycobacterial branched-chain aminotransferase: implications for inhibitor design. Acta Crystallogr D Biol Crystallogr. 2010 May;66(Pt 5):549-57. Epub 2010 Apr 21. PMID:20445230 doi:10.1107/S0907444910004877
- ↑ Tremblay LW, Blanchard JS. The 1.9 A structure of the branched-chain amino-acid transaminase (IlvE) from Mycobacterium tuberculosis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Nov 1;65(Pt, 11):1071-7. Epub 2009 Oct 13. PMID:19923721 doi:10.1107/S1744309109036690
