1o17: Difference between revisions

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-[[Image:1o17.gif|left|200px]]
-<!--
-The line below this paragraph, containing "STRUCTURE_1o17", creates the "Structure Box" on the page.
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-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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-{{STRUCTURE_1o17|  PDB=1o17  |  SCENE=  }}
-'''ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)'''
+==ANTHRANILATE PHOSPHORIBOSYL-TRANSFERASE (TRPD)==
+<StructureSection load='1o17' size='340' side='right'caption='[[1o17]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1o17]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1k8e 1k8e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O17 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O17 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</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=1o17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o17 OCA], [https://pdbe.org/1o17 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o17 RCSB], [https://www.ebi.ac.uk/pdbsum/1o17 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o17 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRPD_SACS2 TRPD_SACS2] Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).[HAMAP-Rule:MF_00211]<ref>PMID:11298741</ref> <ref>PMID:16714288</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o1/1o17_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1o17 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism.
-==Overview==
+Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.,Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M EMBO J. 2002 Jul 1;21(13):3245-54. PMID:12093726<ref>PMID:12093726</ref>
-The crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-O17 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1k8e 1k8e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O17 OCA].
+</div>
+<div class="pdbe-citations 1o17" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry., Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M, EMBO J. 2002 Jul 1;21(13):3245-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12093726 12093726]
+*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
-[[Category: Anthranilate phosphoribosyltransferase]]
+== References ==
-[[Category: Single protein]]
+<references/>
-[[Category: Sulfolobus solfataricus]]
+__TOC__
-[[Category: Ivens, A.]]
+</StructureSection>
-[[Category: Kirschner, K.]]
+[[Category: Large Structures]]
-[[Category: Mayans, O.]]
+[[Category: Saccharolobus solfataricus]]
-[[Category: Wilmanns, M.]]
+[[Category: Ivens A]]
-[[Category: Nucleoside-phosphorylase]]
+[[Category: Kirschner K]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:13:49 2008''
+[[Category: Mayans O]]
+[[Category: Wilmanns M]]