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==Crystal structure of ALD1 from Arabidopsis thaliana== | |||
=== | <StructureSection load='4fl0' size='340' side='right' caption='[[4fl0]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fl0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FL0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FL0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALD1, At2g13810, F13J11.16 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 Arabidopsis thaliana])</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4fl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4fl0 RCSB], [http://www.ebi.ac.uk/pdbsum/4fl0 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:23385743</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Journal:Acta Cryst F:2|Journal:Acta Cryst F:2]] | *[[Journal:Acta Cryst F:2|Journal:Acta Cryst F:2]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Arabidopsis thaliana]] | [[Category: Arabidopsis thaliana]] | ||
[[Category: Albeck, S | [[Category: Albeck, S]] | ||
[[Category: Dym, O | [[Category: Dym, O]] | ||
[[Category: Edelman, M | [[Category: Edelman, M]] | ||
[[Category: Galili, G | [[Category: Galili, G]] | ||
[[Category: ISPC, Israel Structural Proteomics Center | [[Category: ISPC, Israel Structural Proteomics Center]] | ||
[[Category: Kirma, M | [[Category: Kirma, M]] | ||
[[Category: Sobolev, V | [[Category: Sobolev, V]] | ||
[[Category: Unger, T | [[Category: Unger, T]] | ||
[[Category: Pathogen resistance]] | [[Category: Pathogen resistance]] | ||
[[Category: Plp nbinding]] | [[Category: Plp nbinding]] | ||
[[Category: Protein structure initiative]] | [[Category: PSI, Protein structure initiative]] | ||
[[Category: Sandwich fold and architecture]] | [[Category: Sandwich fold and architecture]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 13:39, 21 December 2014
Crystal structure of ALD1 from Arabidopsis thalianaCrystal structure of ALD1 from Arabidopsis thaliana
Structural highlights
Publication Abstract from PubMedDiaminopimelate 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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