1icj

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(New page: 200px<br /><applet load="1icj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1icj, resolution 1.90&Aring;" /> '''PDF PROTEIN IS CRYST...)
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[[Image:1icj.gif|left|200px]]<br /><applet load="1icj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1icj, resolution 1.90&Aring;" />
 
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'''PDF PROTEIN IS CRYSTALLIZED AS NI2+ CONTAINING FORM, COCRYSTALLIZED WITH INHIBITOR POLYETHYLENE GLYCOL (PEG)'''<br />
 
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==Overview==
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==PDF PROTEIN IS CRYSTALLIZED AS NI2+ CONTAINING FORM, COCRYSTALLIZED WITH INHIBITOR POLYETHYLENE GLYCOL (PEG)==
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Peptide deformylase is an essential metalloenzyme required for the removal, of the formyl group at the N terminus of nascent polypeptide chains in, eubacteria. The Escherichia coli enzyme uses Fe2+ and nearly retains its, activity on substitution of the metal ion by Ni2+. We have solved the, structure of the Ni2+ enzyme at 1.9-A resolution by x-ray crystallography., Each of the three monomers in the asymmetric unit contains one Ni2+ ion, and, in close proximity, one molecule of polyethylene glycol. Polyethylene, glycol is shown to be a competitive inhibitor with a KI value of 6 mM with, respect to formylmethionine under conditions similar to those used for, crystallization. We have also solved the structure of the inhibitor-free, enzyme at 2.5-A resolution. The two structures are identical within the, estimated errors of the models. The hydrogen bond network stabilizing the, active site involves nearly all conserved amino acid residues and well, defined water molecules, one of which ligates to the tetrahedrally, coordinated Ni2+ ion.
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<StructureSection load='1icj' size='340' side='right'caption='[[1icj]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1icj]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ICJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ICJ FirstGlance]. <br>
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1ICJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NI, SO4 and 2PE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ICJ OCA].
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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]] 1.9&#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=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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==Reference==
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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=1icj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1icj OCA], [https://pdbe.org/1icj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1icj RCSB], [https://www.ebi.ac.uk/pdbsum/1icj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1icj ProSAT]</span></td></tr>
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Structure of peptide deformylase and identification of the substrate binding site., Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF, J Biol Chem. 1998 May 8;273(19):11413-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9565550 9565550]
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</table>
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[[Category: Escherichia coli]]
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== Function ==
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[[Category: Formylmethionine deformylase]]
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[https://www.uniprot.org/uniprot/DEF_ECOLI DEF_ECOLI] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.[HAMAP-Rule:MF_00163]
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[[Category: Single protein]]
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== Evolutionary Conservation ==
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[[Category: Becker, A.]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Kabsch, W.]]
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Check<jmol>
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[[Category: Schlichting, I.]]
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<jmolCheckbox>
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[[Category: Schultz, S.]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ic/1icj_consurf.spt"</scriptWhenChecked>
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[[Category: Wagner, A.F.V.]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: 2PE]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: NI]]
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</jmolCheckbox>
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[[Category: SO4]]
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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=1icj ConSurf].
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[[Category: hydrolase]]
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<div style="clear:both"></div>
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[[Category: iron metalloprotease]]
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__TOC__
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[[Category: protein synthesis]]
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</StructureSection>
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[[Category: Escherichia coli K-12]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:16:59 2007''
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[[Category: Large Structures]]
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[[Category: Becker A]]
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[[Category: Kabsch W]]
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[[Category: Schlichting I]]
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[[Category: Schultz S]]
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[[Category: Wagner AFV]]

Current revision

PDF PROTEIN IS CRYSTALLIZED AS NI2+ CONTAINING FORM, COCRYSTALLIZED WITH INHIBITOR POLYETHYLENE GLYCOL (PEG)

PDB ID 1icj

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