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1gk1

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[[Image:1gk1.png|left|200px]]
 
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==Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C==
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The line below this paragraph, containing "STRUCTURE_1gk1", creates the "Structure Box" on the page.
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<StructureSection load='1gk1' size='340' side='right'caption='[[1gk1]], [[Resolution|resolution]] 2.40&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'>[[1gk1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GK1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GK1 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]] 2.4&#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=GOL:GLYCEROL'>GOL</scene></td></tr>
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{{STRUCTURE_1gk1| PDB=1gk1 | 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=1gk1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gk1 OCA], [https://pdbe.org/1gk1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gk1 RCSB], [https://www.ebi.ac.uk/pdbsum/1gk1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gk1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/G7AC_PSEU7 G7AC_PSEU7] Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA).<ref>PMID:2993240</ref>
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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/gk/1gk1_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=1gk1 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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Glutarylamidase is an important enzyme employed in the commercial production of 7-aminocephalosporanic acid, a starting compound in the synthesis of cephalosporin antibiotics. 7-aminocephalosporanic acid is obtained from cephalosporin C, a natural antibiotic, either chemically or by a two-step enzymatic process utilizing the enzymes D-amino acid oxidase and glutarylamidase. We have investigated possibilities for redesigning glutarylamidase for the production of 7-aminocephalosporanic acid from cephalosporin C in a single enzymatic step. These studies are based on the structures of glutarylamidase, which we have solved with bound phosphate and ethylene glycol to 2.5 A resolution and with bound glycerol to 2.4 A. The phosphate binds near the catalytic serine in a way that mimics the hemiacetal that develops during catalysis, while the glycerol occupies the side-chain binding pocket. Our structures show that the enzyme is not only structurally similar to penicillin G acylase but also employs essentially the same mechanism in which the alpha-amino group of the catalytic serine acts as a base. A subtle difference is the presence of two catalytic dyads, His B23/Glu B455 and His B23/Ser B1, that are not seen in penicillin G acylase. In contrast to classical serine proteases, the central histidine of these dyads interacts indirectly with the O(gamma) through a hydrogen bond relay network involving the alpha-amino group of the serine and a bound water molecule. A plausible model of the enzyme-substrate complex is proposed that leads to the prediction of mutants of glutarylamidase that should enable the enzyme to deacylate cephalosporin C into 7-aminocephalosporanic acid.
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===STRUCTURE-BASED PREDICTION OF MODIFICATIONS IN GLUTARYLAMIDASE TO ALLOW SINGLE-STEP ENZYMATIC PRODUCTION OF 7-AMINOCEPHALOSPORANIC ACID FROM CEPHALOSPORIN C===
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Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C.,Fritz-Wolf K, Koller KP, Lange G, Liesum A, Sauber K, Schreuder H, Aretz W, Kabsch W Protein Sci. 2002 Jan;11(1):92-103. PMID:11742126<ref>PMID:11742126</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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<div class="pdbe-citations 1gk1" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11742126}}, adds the Publication Abstract to the page
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*[[Cephalosporin acylase 3D structures|Cephalosporin acylase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11742126 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11742126}}
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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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[[1gk1]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GK1 OCA].
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[[Category: Pseudomonas sp]]
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[[Category: Aretz W]]
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==Reference==
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[[Category: Fritz-Wolf K]]
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<ref group="xtra">PMID:011742126</ref><references group="xtra"/>
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[[Category: Kabsch W]]
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[[Category: Penicillin amidase]]
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[[Category: Koller KP]]
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[[Category: Pseudomonas sp.]]
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[[Category: Lange G]]
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[[Category: Aretz, W.]]
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[[Category: Liesum A]]
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[[Category: Fritz-Wolf, K.]]
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[[Category: Sauber K]]
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[[Category: Kabsch, W.]]
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[[Category: Schreuder H]]
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[[Category: Koller, K P.]]
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[[Category: Lange, G.]]
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[[Category: Liesum, A.]]
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[[Category: Sauber, K.]]
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[[Category: Schreuder, H.]]
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[[Category: Catalytic triad]]
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[[Category: Cephalosporin acylase]]
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[[Category: Cephalosporin c]]
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[[Category: Glutaryl acylase]]
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[[Category: Hydrolase]]
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[[Category: Ntn-hydrolase]]
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[[Category: X-raz structure]]
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Current revision

Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C

PDB ID 1gk1

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