|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2jjf' size='340' side='right'caption='[[2jjf]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='2jjf' size='340' side='right'caption='[[2jjf]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jjf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JJF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2JJF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jjf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JJF FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2jje|2jje]], [[2jjg|2jjg]], [[2jjh|2jjh]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/L-lysine_6-transaminase L-lysine 6-transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.36 2.6.1.36] </span></td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jjf OCA], [https://pdbe.org/2jjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jjf RCSB], [https://www.ebi.ac.uk/pdbsum/2jjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jjf ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2jjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jjf OCA], [http://pdbe.org/2jjf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jjf RCSB], [http://www.ebi.ac.uk/pdbsum/2jjf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jjf ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/LAT_MYCTU LAT_MYCTU] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 34: |
Line 35: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: L-lysine 6-transaminase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ramachandran, R]] | |
| - | [[Category: Tripathi, S M]] | |
| - | [[Category: Aminotransferase]] | |
| - | [[Category: Lysine amino transferase]] | |
| | [[Category: Mycobacterium tuberculosis]] | | [[Category: Mycobacterium tuberculosis]] |
| - | [[Category: N328a mutant]] | + | [[Category: Ramachandran R]] |
| - | [[Category: Plp]] | + | [[Category: Tripathi SM]] |
| - | [[Category: Pyridoxal phosphate]]
| + | |
| - | [[Category: Rv3290c]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
LAT_MYCTU
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
Lysine varepsilon-aminotransferase (LAT) converts lysine to alpha-aminoadipate-delta-semialdehyde in a PLP-mediated reaction. We mutated active-site T330, N328 and E243, and structurally rationalized their properties. T330A and T330S mutants cannot bind PLP and are inactive. N328A although inactive, binds to PLP. E243A retains activity, but binds alpha-ketoglutarate in a different conformation. We had earlier identified 2-aminomethyl piperidine derivative as a LAT inhibitor. The co-crystal structure reveals that it mimics binding of C5 substrates and exhibits two binding modes. E243, that shields R422 in the apo enzyme, exhibits conformational changes to permit the binding of the inhibitor in one of the binding modes. Structure-based analysis of bound water in the active site suggests optimization strategies for synthesis of improved inhibitors.
Mutational analysis of Mycobacterium tuberculosis lysine varepsilon-aminotransferase and inhibitor co-crystal structures, reveals distinct binding modes.,Tripathi SM, Agarwal A, Ramachandran R Biochem Biophys Res Commun. 2015 Jul 17-24;463(1-2):154-60. doi:, 10.1016/j.bbrc.2015.05.055. Epub 2015 May 20. PMID:26003725[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tripathi SM, Agarwal A, Ramachandran R. Mutational analysis of Mycobacterium tuberculosis lysine varepsilon-aminotransferase and inhibitor co-crystal structures, reveals distinct binding modes. Biochem Biophys Res Commun. 2015 Jul 17-24;463(1-2):154-60. doi:, 10.1016/j.bbrc.2015.05.055. Epub 2015 May 20. PMID:26003725 doi:http://dx.doi.org/10.1016/j.bbrc.2015.05.055
|
