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1pii

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(New page: 200px<br /><applet load="1pii" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pii, resolution 2.0&Aring;" /> '''THREE-DIMENSIONAL STR...)
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[[Image:1pii.jpg|left|200px]]<br /><applet load="1pii" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pii, resolution 2.0&Aring;" />
 
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'''THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME PHOSPHORIBOSYLANTHRANILATE ISOMERASE: INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM ESCHERICHIA COLI REFINED AT 2.0 ANGSTROMS RESOLUTION'''<br />
 
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==Overview==
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==THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME PHOSPHORIBOSYLANTHRANILATE ISOMERASE: INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM ESCHERICHIA COLI REFINED AT 2.0 ANGSTROMS RESOLUTION==
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The three-dimensional structure of the monomeric bifunctional enzyme, N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate, synthase from Escherichia coli has been refined at 2.0 A resolution, using, oscillation film data obtained from synchrotron radiation. The model, includes the complete protein (452 residues), two phosphate ions and 628, water molecules. The final R-factor is 17.3% for all observed data between, 15 and 2 A resolution. The root-mean-square deviations from ideal bond, lengths and bond angles are 0.010 A and 3.2 degrees, respectively. The, structure of N-(5'-phosphoribosyl)anthranilate isomerase:, indole-3-glycerol-phosphate synthase from E. coli comprises two, beta/alpha-barrel domains that superimpose with a root-mean-square, deviation of 2.03 A for 138 C alpha-pairs. The C-terminal domain (residues, 256 to 452) catalyses the PRAI reaction and the N-terminal domain, (residues 1 to 255) catalyses the IGPS reaction, two sequential steps in, tryptophan biosynthesis. The enzyme has the overall shape of a dumb-bell, resulting in a surface area that is considerably larger than normally, observed for monomeric proteins of this size. The active sites of the PRAI, and the IGPS domains, both located at the C-terminal side of the central, beta-barrel, contain equivalent binding sites for the phosphate moieties, of the substrates N-(5'-phosphoribosyl) anthranilate and, 1-(o-carboxyphenylamino)-1-deoxyribulose-5-phosphate. These two phosphate, binding sites are identical with respect to their positions within the, tertiary structure of the beta/alpha-barrel, the conformation of the, residues involved in phosphate binding and the hydrogen-bonding network, between the phosphate ions and the protein. The active site cavities of, both domains contain similar hydrophobic pockets that presumably bind the, anthranilic acid moieties of the substrates. These similarities of the, tertiary structures and the active sites of the two domains provide, evidence that N-(5'-phosphoribosyl)anthranilate, isomerase:indole-3-glycerol-phosphate synthase from E. coli results from a, gene duplication event of a monomeric beta/alpha-barrel ancestor.
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<StructureSection load='1pii' size='340' side='right'caption='[[1pii]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1pii]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PII FirstGlance]. <br>
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1PII is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Indole-3-glycerol-phosphate_synthase Indole-3-glycerol-phosphate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.48 4.1.1.48] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PII OCA].
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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]] 2&#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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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==Reference==
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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=1pii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pii OCA], [https://pdbe.org/1pii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pii RCSB], [https://www.ebi.ac.uk/pdbsum/1pii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pii ProSAT]</span></td></tr>
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Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution., Wilmanns M, Priestle JP, Niermann T, Jansonius JN, J Mol Biol. 1992 Jan 20;223(2):477-507. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1738159 1738159]
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</table>
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== Function ==
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[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.
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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/pi/1pii_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=1pii ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Indole-3-glycerol-phosphate synthase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Jansonius JN]]
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[[Category: Jansonius, J.N.]]
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[[Category: Priestle JP]]
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[[Category: Priestle, J.P.]]
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[[Category: Wilmanns M]]
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[[Category: Wilmanns, M.]]
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[[Category: PO4]]
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[[Category: bifunctional(isomerase and synthase)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:50:24 2007''
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Current revision

THREE-DIMENSIONAL STRUCTURE OF THE BIFUNCTIONAL ENZYME PHOSPHORIBOSYLANTHRANILATE ISOMERASE: INDOLEGLYCEROLPHOSPHATE SYNTHASE FROM ESCHERICHIA COLI REFINED AT 2.0 ANGSTROMS RESOLUTION

PDB ID 1pii

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