1kgz
From Proteopedia
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==Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase from Erwinia carotovora (current name, Pectobacterium carotovorum)== | ==Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase from Erwinia carotovora (current name, Pectobacterium carotovorum)== | ||
| - | <StructureSection load='1kgz' size='340' side='right' caption='[[1kgz]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='1kgz' size='340' side='right'caption='[[1kgz]], [[Resolution|resolution]] 2.40Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1kgz]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1kgz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KGZ FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PRP:ALPHA-PHOSPHORIBOSYLPYROPHOSPHORIC+ACID'>PRP</scene></td></tr> | |
| - | <tr id=' | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kgz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kgz OCA], [https://pdbe.org/1kgz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kgz RCSB], [https://www.ebi.ac.uk/pdbsum/1kgz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kgz ProSAT]</span></td></tr> |
| - | < | + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/Q8VP84_PECCA Q8VP84_PECCA] 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][SAAS:SAAS00083122] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1kgz ConSurf]. | </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=1kgz ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum has been solved at 2.4 A in complex with Mn(2+)-pyrophosphate, and at 1.9 A without ligands. The enzyme structure has a novel phosphoribosyltransferase (PRT) fold and displays close homology to the structures of pyrimidine nucleoside phosphorylases. The enzyme is a homodimer with a monomer of 345 residues. Each monomer consists of two subdomains, alpha and alpha/beta, which form a cleft containing the active site. The nature of the active site is inferred from the trapped MnPPi complex and detailed knowledge of the active sites of nucleoside phosphorylases. With the anthranilate (An)PRT structure solved, the structures of all the enzymes required for tryptophan biosynthesis are now known. | ||
| - | + | ==See Also== | |
| - | + | *[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]] | |
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| - | == | + | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Pectobacterium carotovorum]] |
| - | [[Category: Edwards | + | [[Category: Edwards S]] |
| - | [[Category: Kim | + | [[Category: Kim C]] |
[[Category: Madhusudan]] | [[Category: Madhusudan]] | ||
| - | [[Category: Mills | + | [[Category: Mills SE]] |
| - | [[Category: Spraggon | + | [[Category: Spraggon G]] |
| - | [[Category: Xuong | + | [[Category: Xuong N-H]] |
| - | [[Category: Yee | + | [[Category: Yee M-C]] |
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Current revision
Crystal Structure Analysis of the Anthranilate Phosphoribosyltransferase from Erwinia carotovora (current name, Pectobacterium carotovorum)
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