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1fm2

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[[Image:1fm2.jpg|left|200px]]
 
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==THE 2 ANGSTROM CRYSTAL STRUCTURE OF CEPHALOSPORIN ACYLASE==
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The line below this paragraph, containing "STRUCTURE_1fm2", creates the "Structure Box" on the page.
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<StructureSection load='1fm2' size='340' side='right'caption='[[1fm2]], [[Resolution|resolution]] 2.00&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'>[[1fm2]] 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=1FM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FM2 FirstGlance]. <br>
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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&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_1fm2| PDB=1fm2 | 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=1fm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fm2 OCA], [https://pdbe.org/1fm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fm2 RCSB], [https://www.ebi.ac.uk/pdbsum/1fm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fm2 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/fm/1fm2_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=1fm2 ConSurf].
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<div style="clear:both"></div>
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'''THE 2 ANGSTROM CRYSTAL STRUCTURE OF CEPHALOSPORIN ACYLASE'''
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==See Also==
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*[[Cephalosporin acylase 3D structures|Cephalosporin acylase 3D structures]]
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== References ==
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==Overview==
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<references/>
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BACKGROUND: Semisynthetic cephalosporins are primarily synthesized from 7-aminocephalosporanic acid (7-ACA), which is usually obtained by chemical deacylation of cephalosporin C (CPC). The chemical production of 7-ACA includes, however, several expensive steps and requires thorough treatment of chemical wastes. Therefore, an enzymatic conversion of CPC to 7-ACA by cephalosporin acylase is of great interest. The biggest obstacle preventing this in industrial production is that cephalosporin acylase uses glutaryl-7ACA as a primary substrate and has low substrate specificity for CPC. RESULTS: We have solved the first crystal structure of a cephalosporin acylase from Pseudomonas diminuta at 2.0 A resolution. The overall structure looks like a bowl with two "knobs" consisting of helix- and strand-rich regions, respectively. The active site is mostly formed by the distinctive structural motif of the N-terminal (Ntn) hydrolase superfamily. Superposition of the 61 residue active-site pocket onto that of penicillin G acylase shows an rmsd in Calpha positions of 1.38 A. This indicates structural similarity in the active site between these two enzymes, but their overall structures are elsewhere quite different. CONCLUSION: The substrate binding pocket of the P. diminuta cephalosporin acylase provides detailed insight into the ten key residues responsible for the specificity of the cephalosporin C side chain in four classes of cephalosporin acylases, and it thereby forms a basis for the design of an enzyme with an improved conversion rate of CPC to 7-ACA. The structure also provides structural evidence that four of the five different classes of cephalosporin acylases can be grouped into one family of the Ntn hydrolase superfamily.
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__TOC__
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</StructureSection>
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==About this Structure==
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1FM2 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=1FM2 OCA].
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==Reference==
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The 2.0 A crystal structure of cephalosporin acylase., Kim Y, Yoon K, Khang Y, Turley S, Hol WG, Structure. 2000 Oct 15;8(10):1059-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11080627 11080627]
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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: Khang, Y.]]
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[[Category: Khang Y]]
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[[Category: Kim, Y.]]
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[[Category: Kim Y]]
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[[Category: Turley, S.]]
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[[Category: Turley S]]
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[[Category: Yoon, K H.]]
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[[Category: Yoon KH]]
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[[Category: Antibiotic]]
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[[Category: Cephalosporin acylase]]
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[[Category: N-terminal hydrolase]]
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[[Category: Penicillin acylase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:29:21 2008''
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THE 2 ANGSTROM CRYSTAL STRUCTURE OF CEPHALOSPORIN ACYLASE

PDB ID 1fm2

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