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[[Image:2ai8.jpg|left|200px]]


{{Structure
==E.coli Polypeptide Deformylase complexed with SB-485343==
|PDB= 2ai8 |SIZE=350|CAPTION= <scene name='initialview01'>2ai8</scene>, resolution 1.700&Aring;
<StructureSection load='2ai8' size='340' side='right'caption='[[2ai8]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SB7:[HYDROXY(3-PHENYLPROPYL)AMINO]METHANOL'>SB7</scene>
<table><tr><td colspan='2'>[[2ai8]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AI8 FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE= def, fms ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SB7:[HYDROXY(3-PHENYLPROPYL)AMINO]METHANOL'>SB7</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ai8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ai8 OCA], [https://pdbe.org/2ai8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ai8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ai8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ai8 ProSAT]</span></td></tr>
|RELATEDENTRY=[[2ai7|2AI7]], [[2ai9|2AI9]], [[2aia|2AIA]], [[2aie|2AIE]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ai8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ai8 OCA], [http://www.ebi.ac.uk/pdbsum/2ai8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ai8 RCSB]</span>
== Function ==
}}
[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]
 
== Evolutionary Conservation ==
'''E.coli Polypeptide Deformylase complexed with SB-485343'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ai/2ai8_consurf.spt"</scriptWhenChecked>
Polypeptide deformylase (PDF) catalyzes the deformylation of polypeptide chains in bacteria. It is essential for bacterial cell viability and is a potential antibacterial drug target. Here, we report the crystal structures of polypeptide deformylase from four different species of bacteria: Streptococcus pneumoniae, Staphylococcus aureus, Haemophilus influenzae, and Escherichia coli. Comparison of these four structures reveals significant overall differences between the two Gram-negative species (E. coli and H. influenzae) and the two Gram-positive species (S. pneumoniae and S. aureus). Despite these differences and low overall sequence identity, the S1' pocket of PDF is well conserved among the four enzymes studied. We also describe the binding of nonpeptidic inhibitor molecules SB-485345, SB-543668, and SB-505684 to both S. pneumoniae and E. coli PDF. Comparison of these structures shows similar binding interactions with both Gram-negative and Gram-positive species. Understanding the similarities and subtle differences in active site structure between species will help to design broad-spectrum polypeptide deformylase inhibitor molecules.
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
2AI8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AI8 OCA].  
</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=2ai8 ConSurf].
 
<div style="clear:both"></div>
==Reference==
__TOC__
Structural variation and inhibitor binding in polypeptide deformylase from four different bacterial species., Smith KJ, Petit CM, Aubart K, Smyth M, McManus E, Jones J, Fosberry A, Lewis C, Lonetto M, Christensen SB, Protein Sci. 2003 Feb;12(2):349-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12538898 12538898]
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Peptide deformylase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Aubart K]]
[[Category: Aubart, K.]]
[[Category: Christensen SB]]
[[Category: Christensen, S B.]]
[[Category: Fosberry A]]
[[Category: Fosberry, A.]]
[[Category: Jones J]]
[[Category: Jones, J.]]
[[Category: Lewis C]]
[[Category: Lewis, C.]]
[[Category: Lonetto M]]
[[Category: Lonetto, M.]]
[[Category: McManus E]]
[[Category: McManus, E.]]
[[Category: Petit CM]]
[[Category: Petit, C M.]]
[[Category: Smith KJ]]
[[Category: Smith, K J.]]
[[Category: Smyth M]]
[[Category: Smyth, M.]]
[[Category: hydrolase]]
 
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