1jw0

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{{Seed}}
 
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[[Image:1jw0.png|left|200px]]
 
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==Structure of cephalosporin acylase in complex with glutarate==
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The line below this paragraph, containing "STRUCTURE_1jw0", creates the "Structure Box" on the page.
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<StructureSection load='1jw0' size='340' side='right'caption='[[1jw0]], [[Resolution|resolution]] 2.50&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'>[[1jw0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JW0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JW0 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]] 2.5&#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=GUA:GLUTARIC+ACID'>GUA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1jw0| PDB=1jw0 | 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=1jw0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jw0 OCA], [https://pdbe.org/1jw0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jw0 RCSB], [https://www.ebi.ac.uk/pdbsum/1jw0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jw0 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/G7AC_BREDI G7AC_BREDI] Catalyzes the deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA). Can not efficiently use cephalosporin C (CPC), penicillin G, or ampicillin as substrates.<ref>PMID:11080627</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/jw/1jw0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1jw0 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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BACKGROUND: Semisynthetic cephalosporins are primarily synthesized from 7-aminocephalosporanic acid (7-ACA), which is obtained by environmentally toxic chemical deacylation of cephalosporin C (CPC). Thus, the enzymatic conversion of CPC to 7-ACA by cephalosporin acylase (CA) would be of great interest. However, CAs use glutaryl-7-ACA (GL-7-ACA) as a primary substrate and the enzyme has low turnover rates for CPC. RESULTS: The binary complex structures of CA with GL-7-ACA and glutarate (the side-chain of GL-7-ACA) show extensive interactions between the glutaryl moiety of GL-7-ACA and the seven residues that form the side-chain pocket. These interactions explain why the D-alpha-aminoadipyl side-chain of CPC yields a poorer substrate than GL-7-ACA. CONCLUSIONS: This understanding of the nature of substrate specificity may be useful in the design of an enzyme with an improved performance for the conversion of CPC to 7-ACA. Additionally, the catalytic mechanism of the deacylation reaction was revealed by the ligand bound structures.
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===Structure of cephalosporin acylase in complex with glutarate===
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Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity.,Kim Y, Hol WG Chem Biol. 2001 Dec;8(12):1253-64. PMID:11755403<ref>PMID:11755403</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 1jw0" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11755403}}, adds the Publication Abstract to the page
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*[[Cephalosporin acylase|Cephalosporin acylase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11755403 is the PubMed ID number.
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*[[Cephalosporin acylase 3D structures|Cephalosporin acylase 3D structures]]
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== References ==
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{{ABSTRACT_PUBMED_11755403}}
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1JW0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Brevundimonas_diminuta Brevundimonas diminuta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JW0 OCA].
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==Reference==
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Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity., Kim Y, Hol WG, Chem Biol. 2001 Dec;8(12):1253-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11755403 11755403]
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[[Category: Brevundimonas diminuta]]
[[Category: Brevundimonas diminuta]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Hol, W G.J.]]
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[[Category: Hol WGJ]]
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[[Category: Kim, Y.]]
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[[Category: Kim Y]]
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[[Category: Cephalosporin acylase]]
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[[Category: Glutarate]]
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[[Category: Glutaryll-7-aca]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 21:03:01 2008''
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Current revision

Structure of cephalosporin acylase in complex with glutarate

PDB ID 1jw0

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