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| | <StructureSection load='4axk' size='340' side='right'caption='[[4axk]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='4axk' size='340' side='right'caption='[[4axk]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4axk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aj_12310 Aj 12310]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AXK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4axk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_efficiens Corynebacterium efficiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AXK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AXK FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 2.25Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1-(5-phosphoribosyl)-5-_((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide_isomerase 1-(5-phosphoribosyl)-5- ((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.16 5.3.1.16] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4axk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4axk OCA], [https://pdbe.org/4axk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4axk RCSB], [https://www.ebi.ac.uk/pdbsum/4axk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4axk ProSAT]</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=4axk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4axk OCA], [https://pdbe.org/4axk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4axk RCSB], [https://www.ebi.ac.uk/pdbsum/4axk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4axk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/HIS4_COREF HIS4_COREF] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aj 12310]] | + | [[Category: Corynebacterium efficiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Barona-Gomez, F]] | + | [[Category: Barona-Gomez F]] |
| - | [[Category: Camacho-Zarco, A R]] | + | [[Category: Camacho-Zarco AR]] |
| - | [[Category: Carrillo-Tripp, M]] | + | [[Category: Carrillo-Tripp M]] |
| - | [[Category: Fulop, V]] | + | [[Category: Fulop V]] |
| - | [[Category: Gaytan, P]] | + | [[Category: Gaytan P]] |
| - | [[Category: Medina-Ruiz, S]] | + | [[Category: Medina-Ruiz S]] |
| - | [[Category: Noda-Garcia, L]] | + | [[Category: Noda-Garcia L]] |
| - | [[Category: Verduzco-Castro, E A]] | + | [[Category: Verduzco-Castro EA]] |
| - | [[Category: Evolution of substrate specificity]]
| + | |
| - | [[Category: Histidine biosynthesis]]
| + | |
| - | [[Category: Isomerase]]
| + | |
| - | [[Category: Metabolism]]
| + | |
| Structural highlights
Function
HIS4_COREF
Publication Abstract from PubMed
Despite the prominent role of horizontal gene transfer (HGT) in shaping bacterial metabolism, little is known about the impact of HGT on the evolution of enzyme function. Specifically, what is the influence of a recently acquired gene on the function of an existing gene? For example, certain members of the genus Corynebacterium have horizontally acquired a whole l-tryptophan biosynthetic operon, whereas in certain closely related actinobacteria, for example, Mycobacterium, the trpF gene is missing. In Mycobacterium, the function of the trpF gene is performed by a dual-substrate (betaalpha)8 phosphoribosyl isomerase (priA gene) also involved in l-histidine (hisA gene) biosynthesis. We investigated the effect of a HGT-acquired TrpF enzyme upon PriA's substrate specificity in Corynebacterium through comparative genomics and phylogenetic reconstructions. After comprehensive in vivo and enzyme kinetic analyses of selected PriA homologs, a novel (betaalpha)8 isomerase subfamily with a specialized function in l-histidine biosynthesis, termed subHisA, was confirmed. X-ray crystallography was used to reveal active-site mutations in subHisA important for narrowing of substrate specificity, which when mutated to the naturally occurring amino acid in PriA led to gain of function. Moreover, in silico molecular dynamic analyses demonstrated that the narrowing of substrate specificity of subHisA is concomitant with loss of ancestral protein conformational states. Our results show the importance of HGT in shaping enzyme evolution and metabolism.
Evolution of substrate specificity in a recipient's enzyme following horizontal gene transfer.,Noda-Garcia L, Camacho-Zarco AR, Medina-Ruiz S, Gaytan P, Carrillo-Tripp M, Fulop V, Barona-Gomez F Mol Biol Evol. 2013 Sep;30(9):2024-34. doi: 10.1093/molbev/mst115. Epub 2013 Jun , 25. PMID:23800623[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Noda-Garcia L, Camacho-Zarco AR, Medina-Ruiz S, Gaytan P, Carrillo-Tripp M, Fulop V, Barona-Gomez F. Evolution of substrate specificity in a recipient's enzyme following horizontal gene transfer. Mol Biol Evol. 2013 Sep;30(9):2024-34. doi: 10.1093/molbev/mst115. Epub 2013 Jun , 25. PMID:23800623 doi:http://dx.doi.org/10.1093/molbev/mst115
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