1hjf

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[[Image:1hjf.png|left|200px]]
 
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==Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase: The role of arginine-258==
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The line below this paragraph, containing "STRUCTURE_1hjf", creates the "Structure Box" on the page.
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<StructureSection load='1hjf' size='340' side='right'caption='[[1hjf]], [[Resolution|resolution]] 1.60&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'>[[1hjf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HJF 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]] 1.6&#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=COI:2-OXO-4-METHYLPENTANOIC+ACID'>COI</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
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{{STRUCTURE_1hjf| PDB=1hjf | 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=1hjf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjf OCA], [https://pdbe.org/1hjf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hjf RCSB], [https://www.ebi.ac.uk/pdbsum/1hjf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hjf ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CEFE_STRCL CEFE_STRCL] Catalyzes the step from penicillin N to deacetoxy-cephalosporin C.
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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/hj/1hjf_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=1hjf 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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Deacetoxycephalosporin C synthase is an iron(II) 2-oxoglutaratedependent oxygenase that catalyzes the oxidative ring-expansion of penicillin N to deacetoxycephalosporin C. The wild-type enzyme is only able to efficiently utilize 2-oxoglutarate and 2-oxoadipate as a 2-oxoacid co-substrate. Mutation of arginine 258, the side chain of which forms an electrostatic interaction with the 5-carboxylate of the 2-oxoglutarate co-substrate, to a glutamine residue reduced activity to about 5% of the wild-type enzyme with 2-oxoglutarate. However, other aliphatic 2-oxoacids, which were not co-substrates for the wild-type enzyme, were utilized by the R258Q mutant. These 2-oxoacids "rescued" catalytic activity to the level observed for the wild-type enzyme as judged by penicillin N and G conversion. These co-substrates underwent oxidative decarboxylation as observed for 2-oxoglutarate in the normal reaction with the wild-type enzyme. Crystal structures of the iron(II)- 2-oxo-3-methylbutanoate (1.5 A), and iron(II)-2-oxo-4-methylpentanoate (1.6 A) enzyme complexes were obtained, which reveal the molecular basis for this "chemical co-substrate rescue" and help to rationalize the co-substrate selectivity of 2-oxoglutaratedependent oxygenases.
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===ALTERATION OF THE CO-SUBSTRATE SELECTIVITY OF DEACETOXYCEPHALOSPORIN C SYNTHASE: THE ROLE OF ARGININE-258===
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Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase. The role of arginine 258.,Lee HJ, Lloyd MD, Clifton IJ, Harlos K, Dubus A, Baldwin JE, Frere JM, Schofield CJ J Biol Chem. 2001 May 25;276(21):18290-5. Epub 2001 Feb 21. PMID:11279000<ref>PMID:11279000</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_11279000}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1hjf" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11279000 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11279000}}
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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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[[1hjf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_clavuligerus Streptomyces clavuligerus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJF OCA].
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==Reference==
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<ref group="xtra">PMID:11279000</ref><ref group="xtra">PMID:10222202</ref><references group="xtra"/>
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[[Category: Streptomyces clavuligerus]]
[[Category: Streptomyces clavuligerus]]
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[[Category: Baldwin, J E.]]
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[[Category: Baldwin JE]]
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[[Category: Clifton, I J.]]
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[[Category: Clifton IJ]]
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[[Category: Dubus, A.]]
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[[Category: Dubus A]]
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[[Category: Frere, J M.]]
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[[Category: Frere JM]]
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[[Category: Harlos, K.]]
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[[Category: Harlos K]]
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[[Category: Lee, H J.]]
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[[Category: Lee HJ]]
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[[Category: Lloyd, M D.]]
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[[Category: Lloyd MD]]
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[[Category: Schofield, C J.]]
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[[Category: Schofield CJ]]
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[[Category: 2- oxoglutarate-dependent oxygenase]]
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[[Category: Alternative 2-oxoacid]]
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[[Category: Cephem antibiotic biosynthesis]]
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[[Category: Chemical cosubstrate rescue]]
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[[Category: Co-substrate selectivity]]
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[[Category: Oxidoreductase]]
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Current revision

Alteration of the co-substrate selectivity of deacetoxycephalosporin C synthase: The role of arginine-258

PDB ID 1hjf

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