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| | <StructureSection load='4wb0' size='340' side='right'caption='[[4wb0]], [[Resolution|resolution]] 1.91Å' scene=''> | | <StructureSection load='4wb0' size='340' side='right'caption='[[4wb0]], [[Resolution|resolution]] 1.91Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4wb0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leime Leime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WB0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WB0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4wb0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WB0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></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=4wb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wb0 OCA], [https://pdbe.org/4wb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wb0 RCSB], [https://www.ebi.ac.uk/pdbsum/4wb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wb0 ProSAT]</span></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=4wb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wb0 OCA], [http://pdbe.org/4wb0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wb0 RCSB], [http://www.ebi.ac.uk/pdbsum/4wb0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wb0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q71PB4_LEIME Q71PB4_LEIME] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Leime]] | + | [[Category: Leishmania mexicana]] |
| - | [[Category: Blankenfeldt, W]] | + | [[Category: Blankenfeldt W]] |
| - | [[Category: Nowicki, C]] | + | [[Category: Nowicki C]] |
| - | [[Category: Wen, J]] | + | [[Category: Wen J]] |
| - | [[Category: Broad specificity]]
| + | |
| - | [[Category: Pyridoxal phosphate]]
| + | |
| - | [[Category: Transamination]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q71PB4_LEIME
Publication Abstract from PubMed
Leishmania species are early branching eukaryotic parasites that cause difficult-to-treat tissue-damaging diseases known as leishmaniases. As a hallmark of their parasitic lifestyle, Leishmaniae express a number of aminotransferases that are involved in important cellular processes and exhibit broader substrate specificity than their mammalian host's counterparts. Here, we have determined the crystal structure of the broad specificity aminotransferase from Leishmania mexicana (LmexBSAT) at 1.91A resolution. LmexBSAT is a homodimer and belongs to the alpha-branch of family-I aminotransferases. Despite the fact that the protein was crystallized in the absence of substrates and has lost the pyridoxal-5'-phosphate (PLP) cofactor during crystallization, the structure resembles the closed, ligand-bound form of related enzymes such as chicken cytosolic aspartate aminotransferase. Its broader substrate specificity seems to be rooted in increased flexibility of a substrate-binding arginine (R291) and the interactions of this residue with the N-terminus of the second chain of the dimer.
Structural basis for the relaxed substrate selectivity of Leishmania mexicana broad specificity aminotransferase.,Wen J, Nowicki C, Blankenfeldt W Mol Biochem Parasitol. 2015 Aug;202(2):34-7. doi:, 10.1016/j.molbiopara.2015.09.007. Epub 2015 Oct 8. PMID:26456583[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wen J, Nowicki C, Blankenfeldt W. Structural basis for the relaxed substrate selectivity of Leishmania mexicana broad specificity aminotransferase. Mol Biochem Parasitol. 2015 Aug;202(2):34-7. doi:, 10.1016/j.molbiopara.2015.09.007. Epub 2015 Oct 8. PMID:26456583 doi:http://dx.doi.org/10.1016/j.molbiopara.2015.09.007
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