2x30

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[[Image:2x30.png|left|200px]]
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==CRYSTAL STRUCTURE OF THE R139N MUTANT OF A BIFUNCTIONAL ENZYME PRIA==
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<StructureSection load='2x30' size='340' side='right' caption='[[2x30]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2x30]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X30 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vep|2vep]], [[1vzw|1vzw]]</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x30 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x30 RCSB], [http://www.ebi.ac.uk/pdbsum/2x30 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x3/2x30_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A good model to experimentally explore evolutionary hypothesis related to enzyme function is the ancient-like dual-substrate (betaalpha)(8) phosphoribosyl isomerase (PriA), which takes part in both histidine and tryptophan biosynthesis in Streptomyces coelicolor and related organisms. In this study, we determined the Michaelis - Menten enzyme kinetics for both isomerase activities in wild-type PriA from S. coelicolor, as well as in selected single-residue mono-functional mutants, identified after Escherichia coli in vivo complementation experiments. Structural and functional analyses of a hitherto unnoticed residue contained on the functionally important beta --&gt; alpha loop 5, namely, Arg(139), which was postulated on structural grounds to be important for the dual-substrate specificity of PriA, is presented for the first time. Indeed, enzyme kinetics analyses done on the mutant variants PriA_Ser(81)Thr and PriA_Arg(139)Asn showed that these residues, which are contained on beta --&gt; alpha loops and in close proximity to the N-terminal phosphate-binding site, are essential solely for the phosphoribosyl anthranilate isomerase activity of PriA. Moreover, analysis of the X-ray crystallographic structure of PriA_Arg(139)Asn elucidated at 1.95 A herein, strongly implicates the occurrence of conformational changes in this beta --&gt; alpha loop as a major structural feature related to the evolution of the dual-substrate specificity of PriA. It is suggested that PriA has evolved by tuning a fine energetic balance that allows the sufficient degree of structural flexibility needed for accommodating two topologically dissimilar substrates - within a bifunctional and thus highly constrained active site - without compromising its structural stability.
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{{STRUCTURE_2x30| PDB=2x30 | SCENE= }}
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Identification and analysis of residues contained on beta --&gt; alpha loops of the dual-substrate (betaalpha)(8) phosphoribosyl isomerase a (PriA) specific for its phosphoribosyl anthranilate isomerase activity.,Noda-Garcia L, Camacho-Zarco AR, Verdel-Aranda K, Wright H, Soberon X, Fulop V, Barona-Gomez F Protein Sci. 2010 Jan 11. PMID:20066665<ref>PMID:20066665</ref>
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===CRYSTAL STRUCTURE OF THE R139N MUTANT OF A BIFUNCTIONAL ENZYME PRIA===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_20066665}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[2x30]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X30 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:020066665</ref><references group="xtra"/>
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[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
[[Category: Barona-Gomez, F.]]
[[Category: Barona-Gomez, F.]]

Revision as of 01:23, 1 October 2014

CRYSTAL STRUCTURE OF THE R139N MUTANT OF A BIFUNCTIONAL ENZYME PRIA

2x30, resolution 1.95Å

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