1khd: Difference between revisions

New page: left|200px<br /><applet load="1khd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1khd, resolution 1.86Å" /> '''Crystal Structure An...
 
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'''Crystal Structure Analysis of the anthranilate phosphoribosyltransferase from Erwinia carotovora at 1.9 resolution (current name, Pectobacterium carotovorum)'''<br />


==Overview==
==Crystal Structure Analysis of the anthranilate phosphoribosyltransferase from Erwinia carotovora at 1.9 resolution (current name, Pectobacterium carotovorum)==
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.
<StructureSection load='1khd' size='340' side='right'caption='[[1khd]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1khd]] is a 4 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=1KHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KHD 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]] 1.86&#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=1khd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1khd OCA], [https://pdbe.org/1khd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1khd RCSB], [https://www.ebi.ac.uk/pdbsum/1khd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1khd ProSAT]</span></td></tr>
</table>
== 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 ==
[[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/kh/1khd_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=1khd ConSurf].
<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.


==About this Structure==
The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum.,Kim C, Xuong NH, Edwards S, Madhusudan, Yee MC, Spraggon G, Mills SE FEBS Lett. 2002 Jul 17;523(1-3):239-46. PMID:12123839<ref>PMID:12123839</ref>
1KHD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pectobacterium_carotovorum Pectobacterium carotovorum]. Active as [http://en.wikipedia.org/wiki/Anthranilate_phosphoribosyltransferase Anthranilate phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.18 2.4.2.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KHD OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum., Kim C, Xuong NH, Edwards S, Madhusudan, Yee MC, Spraggon G, Mills SE, FEBS Lett. 2002 Jul 17;523(1-3):239-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12123839 12123839]
</div>
[[Category: Anthranilate phosphoribosyltransferase]]
<div class="pdbe-citations 1khd" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pectobacterium carotovorum]]
[[Category: Pectobacterium carotovorum]]
[[Category: Single protein]]
[[Category: Edwards S]]
[[Category: Edwards, S.]]
[[Category: Kim C]]
[[Category: Kim, C.]]
[[Category: Madhusudan]]
[[Category: Madhusudan]]
[[Category: Mills, S.E.]]
[[Category: Mills SE]]
[[Category: Spraggon, G.]]
[[Category: Spraggon G]]
[[Category: Xuong, N.H.]]
[[Category: Xuong N-H]]
[[Category: Yee, M.C.]]
[[Category: Yee M-C]]
[[Category: nucleotide binding fold]]
[[Category: type 3 prt fold]]
 
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