4tx9: Difference between revisions
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==Crystal structure of HisAp from Streptomyces sviceus with degraded ProFAR== | ==Crystal structure of HisAp from Streptomyces sviceus with degraded ProFAR== | ||
<StructureSection load='4tx9' size='340' side='right' caption='[[4tx9]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4tx9' size='340' side='right'caption='[[4tx9]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4tx9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TX9 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4tx9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sviceus_ATCC_29083 Streptomyces sviceus ATCC 29083]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TX9 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
<tr><td class="sblockLbl"><b>[[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMZ:AMINOIMIDAZOLE+4-CARBOXAMIDE+RIBONUCLEOTIDE'>AMZ</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tx9 OCA], [https://pdbe.org/4tx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tx9 RCSB], [https://www.ebi.ac.uk/pdbsum/4tx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tx9 ProSAT]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/B5I4P8_STRX2 B5I4P8_STRX2] Involved in both the histidine and tryptophan biosynthetic pathways.[HAMAP-Rule:MF_01014] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We investigate the evolution of co-occurring analogous enzymes involved in L-tryptophan and L-histidine biosynthesis in Actinobacteria Phylogenetic analysis of trpF homologues, a missing gene in certain clades of this lineage whose absence is complemented by a dual-substrate HisA homologue, termed PriA, found that they fall into three categories: (i) trpF-1, an L-tryptophan biosynthetic gene horizontally acquired by certain Corynebacterium species; (ii) trpF-2, a paralogue known to be involved in synthesizing a pyrrolopyrrole moiety and (iii) trpF-3, a variable non-conserved orthologue of trpF-1 We previously investigated the effect of trpF-1 upon the evolution of PriA substrate specificity, but nothing is known about the relationship between trpF-3 and priA After in vitro steady-state enzyme kinetics we found that trpF-3 encodes a phosphoribosyl anthranilate isomerase. However, mutation of this gene in Streptomyces sviceus did not lead to auxothrophy, as expected from the biosynthetic role of trpF-1 Biochemical characterization of a dozen co-occurring TrpF-2 or TrpF-3, with PriA homologues, explained the prototrophic phenotype, and unveiled an enzyme activity trade-off between TrpF and PriA. X-ray structural analysis suggests that the function of these PriA homologues is mediated by non-conserved mutations in the flexible L5 loop, which may be responsible for different substrate affinities. Thus, the PriA homologues that co-occur with TrpF-3 represent a novel enzyme family, termed PriB, which evolved in response to PRA isomerase activity. The characterization of co-occurring enzymes provides insights into the influence of functional redundancy on the evolution of enzyme function, which could be useful for enzyme functional annotation. | |||
Co-occurrence of analogous enzymes determines evolution of a novel (betaalpha)8-isomerase sub-family after non-conserved mutations in flexible loop.,Verduzco-Castro EA, Michalska K, Endres M, Juarez-Vazquez AL, Noda-Garcia L, Chang C, Henry CS, Babnigg G, Joachimiak A, Barona-Gomez F Biochem J. 2016 May 1;473(9):1141-52. doi: 10.1042/BJ20151271. Epub 2016 Feb 29. PMID:26929404<ref>PMID:26929404</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4tx9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Streptomyces sviceus ATCC 29083]] | ||
[[Category: | [[Category: Barona-Gomez F]] | ||
[[Category: | [[Category: Endres M]] | ||
[[Category: | [[Category: Joachimiak A]] | ||
[[Category: Michalska K]] | |||
[[Category: | [[Category: Verduzco-Castro EA]] | ||
[[Category: | |||
