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3bf7

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[[Image:3bf7.jpg|left|200px]]
 
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{{Structure
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==1.1 resolution structure of ybfF, a new esterase from Escherichia coli: a unique substrate-binding crevice generated by domain arrangement==
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|PDB= 3bf7 |SIZE=350|CAPTION= <scene name='initialview01'>3bf7</scene>, resolution 1.1&Aring;
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<StructureSection load='3bf7' size='340' side='right'caption='[[3bf7]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[3bf7]] is a 2 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=3BF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BF7 FirstGlance]. <br>
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|ACTIVITY=
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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]] 1.1&#8491;</td></tr>
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|GENE= K12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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=3bf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bf7 OCA], [https://pdbe.org/3bf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bf7 RCSB], [https://www.ebi.ac.uk/pdbsum/3bf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bf7 ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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'''1.1 resolution structure of ybfF, a new esterase from Escherichia coli: a unique substrate-binding crevice generated by domain arrangement'''
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[https://www.uniprot.org/uniprot/YBFF_ECOLI YBFF_ECOLI] Displays esterase activity toward palmitoyl-CoA, malonyl-CoA and pNP-butyrate.<ref>PMID:15808744</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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==Overview==
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Check<jmol>
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Esterases are one of the most common enzymes and are involved in diverse cellular functions. ybfF protein from Escherichia coli (Ec_ybfF) belongs to the esterase family for the large substrates, palmitoyl coenzyme A and malonyl coenzyme A, which are important cellular intermediates for energy conversion and biomolecular synthesis. To obtain molecular information on ybfF esterase, which is found in a wide range of microorganisms, we elucidated the crystal structures of Ec_ybfF in complexes with small molecules at resolutions of 1.1 and 1.68 A, respectively. The structure of Ec_ybfF is composed of a globular alpha/beta hydrolase domain with a three-helical bundle cap, which is linked by a kinked helix to the alpha/beta hydrolase domain. It contains a catalytic tetrad of Ser-His-Asp-Ser with the first Ser acting as a nucleophile. The unique spatial arrangement and orientation of the helical cap with respect to the alpha/beta hydrolase domain form a substrate-binding crevice for large substrates. The helical cap is also directly involved in catalysis by providing a substrate anchor, viz., the conserved residues of Arg123 and Tyr208. The high-resolution structure of Ec_ybfF shows that the inserted helical bundle structure and its spatial orientation with respect to the alpha/beta hydrolase domain are critical for creating a large inner space and constituting a specific active site, thereby providing the broad substrate spectrum toward large biomolecules.
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/3bf7_consurf.spt"</scriptWhenChecked>
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==About this Structure==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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3BF7 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=3BF7 OCA].
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==Reference==
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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=3bf7 ConSurf].
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High-resolution structure of ybfF from Escherichia coli K12: a unique substrate-binding crevice generated by domain arrangement., Park SY, Lee SH, Lee J, Nishi K, Kim YS, Jung CH, Kim JS, J Mol Biol. 2008 Mar 7;376(5):1426-37. Epub 2008 Jan 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18215690 18215690]
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Kim, J S.]]
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[[Category: Kim JS]]
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[[Category: Park, S K.]]
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[[Category: Park SK]]
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[[Category: esterase]]
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[[Category: helical cap]]
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[[Category: hydrolase]]
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[[Category: thioesterase]]
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[[Category: ybff]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:58:30 2008''
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Current revision

1.1 resolution structure of ybfF, a new esterase from Escherichia coli: a unique substrate-binding crevice generated by domain arrangement

PDB ID 3bf7

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