2x30

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{{Seed}}
 
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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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The line below this paragraph, containing "STRUCTURE_2x30", creates the "Structure Box" on the page.
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<StructureSection load='2x30' size='340' side='right'caption='[[2x30]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2x30]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2X30 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2x30| PDB=2x30 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2x30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x30 OCA], [https://pdbe.org/2x30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x30 RCSB], [https://www.ebi.ac.uk/pdbsum/2x30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x30 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HIS4_STRCO HIS4_STRCO] Catalyzes the isomerization of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR in the biosynthesis pathway for histidine and the isomerization of the aminoaldose PRA to the aminoketose CdRP in the biosynthsis pathway for tryptophan.[HAMAP-Rule:MF_01014]
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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/main_output.php?pdb_ID=2x30 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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===CRYSTAL STRUCTURE OF THE R139N MUTANT OF A BIFUNCTIONAL ENZYME PRIA===
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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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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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The line below this paragraph, {{ABSTRACT_PUBMED_20066665}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2x30" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20066665 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20066665}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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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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==Reference==
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<ref group="xtra">PMID:20066665</ref><references group="xtra"/>
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[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
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[[Category: Barona-Gomez, F.]]
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[[Category: Barona-Gomez F]]
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[[Category: Camacho-Zarco, A R.]]
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[[Category: Camacho-Zarco AR]]
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[[Category: Fulop, V.]]
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[[Category: Fulop V]]
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[[Category: Noda-Garcia, L.]]
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[[Category: Noda-Garcia L]]
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[[Category: Soberon, X.]]
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[[Category: Soberon X]]
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[[Category: Verdel-Aranda, K.]]
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[[Category: Verdel-Aranda K]]
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[[Category: Wright, H.]]
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[[Category: Wright H]]
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[[Category: Aromatic amino acid biosynthesis]]
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[[Category: Conformational diversity]]
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[[Category: Dual-substrate specificity]]
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[[Category: Hisa]]
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[[Category: Histidine biosynthesis]]
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[[Category: Isomerase]]
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[[Category: Loops motion]]
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[[Category: Trpf]]
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[[Category: Tryptophan biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 26 08:37:48 2010''
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Current revision

Crystal structure of the r139n mutant of a bifunctional enzyme pria

PDB ID 2x30

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