4fl0

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Crystal structure of ALD1 from Arabidopsis thalianaCrystal structure of ALD1 from Arabidopsis thaliana

Structural highlights

4fl0 is a 2 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:ALD1, At2g13810, F13J11.16 (ARATH)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ALD1_ARATH] Aminotransferase involved in local and systemic acquired resistance (SAR) to the bacterial pathogen P.syringae. Required for salicylic acid (SA) and camalexin accumulation upon pathogen infection. Possesses aminotransferase activity in vitro and may generate amino-acid-derived defense signals in vivo. May be involved in ethylene-induced senescence signaling.[1] [2] [3] [4] [5]

Publication Abstract from PubMed

Diaminopimelate aminotransferase (DAP-AT) is an enzyme in the lysine-biosynthesis pathway. Conversely, ALD1, a close homologue of DAP-AT in plants, uses lysine as a substrate in vitro. Both proteins require pyridoxal-5'-phosphate (PLP) for their activity. The structure of ALD1 from the flowering plant Arabidopsis thaliana (AtALD1) was solved at a resolution of 2.3 A. Comparison of AtALD1 with the previously solved structure of A. thaliana DAP-AT (AtDAP-AT) revealed similar interactions with PLP despite sequence differences within the PLP-binding site. However, sequence differences between the binding site of AtDAP-AT for malate, a purported mimic of substrate binding, and the corresponding site in AtALD1 led to different interactions. This suggests that either the substrate itself, or the substrate-binding mode, differs in the two proteins, supporting the known in vitro findings.

Structure of ALD1, a plant-specific homologue of the universal diaminopimelate aminotransferase enzyme of lysine biosynthesis.,Sobolev V, Edelman M, Dym O, Unger T, Albeck S, Kirma M, Galili G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Feb 1;69(Pt 2):84-9. doi: , 10.1107/S1744309112050270. Epub 2013 Jan 26. PMID:23385743[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Song JT, Lu H, Greenberg JT. Divergent roles in Arabidopsis thaliana development and defense of two homologous genes, aberrant growth and death2 and AGD2-LIKE DEFENSE RESPONSE PROTEIN1, encoding novel aminotransferases. Plant Cell. 2004 Feb;16(2):353-66. Epub 2004 Jan 16. PMID:14729919 doi:10.1105/tpc.019372
  2. ↑ Song JT, Lu H, McDowell JM, Greenberg JT. A key role for ALD1 in activation of local and systemic defenses in Arabidopsis. Plant J. 2004 Oct;40(2):200-12. PMID:15447647 doi:10.1111/j.1365-313X.2004.02200.x
  3. ↑ Zhang Z, Lenk A, Andersson MX, Gjetting T, Pedersen C, Nielsen ME, Newman MA, Hou BH, Somerville SC, Thordal-Christensen H. A lesion-mimic syntaxin double mutant in Arabidopsis reveals novel complexity of pathogen defense signaling. Mol Plant. 2008 May;1(3):510-27. doi: 10.1093/mp/ssn011. Epub 2008 Apr 15. PMID:19825557 doi:10.1093/mp/ssn011
  4. ↑ Lee MW, Jelenska J, Greenberg JT. Arabidopsis proteins important for modulating defense responses to Pseudomonas syringae that secrete HopW1-1. Plant J. 2008 May;54(3):452-65. doi: 10.1111/j.1365-313X.2008.03439.x. Epub 2008 , Feb 7. PMID:18266921 doi:10.1111/j.1365-313X.2008.03439.x
  5. ↑ Nie H, Wu Y, Yao C, Tang D. Suppression of edr2-mediated powdery mildew resistance, cell death and ethylene-induced senescence by mutations in ALD1 in Arabidopsis. J Genet Genomics. 2011 Apr 20;38(4):137-48. doi: 10.1016/j.jgg.2011.03.001. Epub , 2011 Mar 23. PMID:21530897 doi:10.1016/j.jgg.2011.03.001
  6. ↑ Sobolev V, Edelman M, Dym O, Unger T, Albeck S, Kirma M, Galili G. Structure of ALD1, a plant-specific homologue of the universal diaminopimelate aminotransferase enzyme of lysine biosynthesis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Feb 1;69(Pt 2):84-9. doi: , 10.1107/S1744309112050270. Epub 2013 Jan 26. PMID:23385743 doi:10.1107/S1744309112050270

4fl0, resolution 2.30Å

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