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| | ==Three-dimensional structure of a truncated phosphoribosylanthranilate isomerase (residues 255-384) from Escherichia coli== | | ==Three-dimensional structure of a truncated phosphoribosylanthranilate isomerase (residues 255-384) from Escherichia coli== |
| - | <StructureSection load='2kzh' size='340' side='right' caption='[[2kzh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kzh' size='340' side='right'caption='[[2kzh]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kzh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KZH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kzh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KZH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KZH FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1pii|1pii]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpC, b1262, JW1254 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=2kzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kzh OCA], [https://pdbe.org/2kzh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kzh RCSB], [https://www.ebi.ac.uk/pdbsum/2kzh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kzh ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoribosylanthranilate_isomerase Phosphoribosylanthranilate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.24 5.3.1.24] </span></td></tr>
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| - | <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=2kzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kzh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kzh RCSB], [http://www.ebi.ac.uk/pdbsum/2kzh PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/TRPC_ECOLI TRPC_ECOLI] Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 2kzh" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Phosphoribosylanthranilate isomerase]] | + | [[Category: Large Structures]] |
| - | [[Category: Mackay, J P]] | + | [[Category: Mackay JP]] |
| - | [[Category: Patrick, W M]] | + | [[Category: Patrick WM]] |
| - | [[Category: Setiyaputra, S]] | + | [[Category: Setiyaputra S]] |
| - | [[Category: Isomerase]]
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| - | [[Category: Protein evolution]]
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| - | [[Category: Subdomain]]
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| - | [[Category: Tim-barrel]]
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| - | [[Category: Tryptophan biosynthesis]]
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| Structural highlights
Function
TRPC_ECOLI Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain.
Publication Abstract from PubMed
The (betaalpha)(8) barrel is one of the most common protein folds, and enzymes with this architecture display a remarkable range of catalytic activities. Many of these functions are associated with ancient metabolic pathways, and phylogenetic reconstructions suggest that the (betaalpha)(8) barrel was one of the very first protein folds to emerge. Consequently, there is considerable interest in understanding the evolutionary processes that gave rise to this fold. In particular, much attention has been focused on the plausibility of (betaalpha)(8) barrel evolution from homodimers of half barrels. However, we previously isolated a three-quarter-barrel-sized fragment of a (betaalpha)(8) barrel, termed truncated phosphoribosylanthranilate isomerase (trPRAI), that is soluble and almost as thermostable as full-length N-(5'-phosphoribosyl)anthranilate isomerase (PRAI). Here, we report the NMR-derived structure of trPRAI. The subdomain is monomeric, is well ordered and adopts a native-like structure in solution. Side chains from strands beta(1) (Glu3 and Lys5), beta(2) (Tyr25) and beta(6) (Lys122) of trPRAI repack to shield the hydrophobic core from the solvent. This result demonstrates that three-quarter barrels were viable intermediates in the evolution of the (betaalpha)(8) barrel fold. We propose a unified model for (betaalpha)(8) barrel evolution that combines our data, previously published work and plausible scenarios for the emergence of (initially error-prone) genetic systems. In this model, the earliest proto-cells contained diverse pools of part-barrel subdomains. Combinatorial assembly of these subdomains gave rise to many distinct lineages of (betaalpha)(8) barrel proteins, that is, our model excludes the possibility that there was a single (betaalpha)(8) barrel from which all present examples are descended.
The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the (betaalpha)8 barrel fold.,Setiyaputra S, Mackay JP, Patrick WM J Mol Biol. 2011 Apr 29;408(2):291-303. Epub 2011 Feb 25. PMID:21354426[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Setiyaputra S, Mackay JP, Patrick WM. The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the (betaalpha)8 barrel fold. J Mol Biol. 2011 Apr 29;408(2):291-303. Epub 2011 Feb 25. PMID:21354426 doi:10.1016/j.jmb.2011.02.048
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