1vzw

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{{Seed}}
 
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[[Image:1vzw.png|left|200px]]
 
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==Crystal structure of the bifunctional protein Pria==
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The line below this paragraph, containing "STRUCTURE_1vzw", creates the "Structure Box" on the page.
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<StructureSection load='1vzw' size='340' side='right'caption='[[1vzw]], [[Resolution|resolution]] 1.80&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'>[[1vzw]] 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=1VZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VZW 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]] 1.8&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1vzw| PDB=1vzw | 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=1vzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vzw OCA], [https://pdbe.org/1vzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vzw RCSB], [https://www.ebi.ac.uk/pdbsum/1vzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vzw 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/vz/1vzw_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=1vzw 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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Some bacterial genomes contain an incomplete set of genes encoding phosphoribosyl isomerases, raising the question of whether there exists broadened substrate specificity for the missing gene products. To investigate the underlying molecular principles of this hypothesis, we have determined the crystal structure of the bifunctional enzyme PriA from Streptomyces coelicolor at 1.8 A resolution. It consists of a (betaalpha)(8)-barrel fold that is assembled by two symmetric (betaalpha)(4) half-barrels. The structure shows how its active site may catalyse the isomerization reactions of two different substrates, and we provide a plausible model of how the smaller of the two substrates could be bound in two different orientations. Our findings expand the half-barrel ancestor concept by demonstrating that symmetry-related half-barrels could provide a smart solution to cope with dual substrate specificity. The data may help to unravel molecular rationales regarding how organisms with miniature genomes can keep central biological pathways functional.
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===CRYSTAL STRUCTURE OF THE BIFUNCTIONAL PROTEIN PRIA===
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Two-fold repeated (betaalpha)4 half-barrels may provide a molecular tool for dual substrate specificity.,Kuper J, Doenges C, Wilmanns M EMBO Rep. 2005 Feb;6(2):134-9. PMID:15654319<ref>PMID:15654319</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_15654319}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1vzw" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15654319 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15654319}}
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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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1VZW is a 1 chain structure of 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=1VZW OCA].
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==Reference==
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<ref group="xtra">PMID:15654319</ref><references group="xtra"/>
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[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
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[[Category: Kuper, J.]]
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[[Category: Kuper J]]
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[[Category: Wilmanns, M.]]
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[[Category: Wilmanns M]]
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[[Category: Histidine biosynthesis]]
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[[Category: Isomerase]]
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[[Category: Tryptophan biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 20:37:12 2009''
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Current revision

Crystal structure of the bifunctional protein Pria

PDB ID 1vzw

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